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| OPM protein=
| OPM protein=
| PDB=
| PDB=
{{PDB3|1wip}}A:317-388 {{PDB3|1wiq}}B:317-388 {{PDB3|1wio}}B:317-388
{{PDB3|1wip}}A:317–388 {{PDB3|1wiq}}B:317–388 {{PDB3|1wio}}B:317–388
{{PDB3|1cid}} :316-386 {{PDB3|1hng}}B:128-198 {{PDB3|1hnf}} :135-205
{{PDB3|1cid}} :316–386 {{PDB3|1hng}}B:128–198 {{PDB3|1hnf}} :135–205
{{PDB3|1rzk}}C:125-203 {{PDB3|1gc1}}C:125-203 {{PDB3|1cdi}} :125-203
{{PDB3|1rzk}}C:125–203 {{PDB3|1gc1}}C:125–203 {{PDB3|1cdi}} :125–203
{{PDB3|2b4c}}C:125-203 {{PDB3|1g9n}}C:125-203 {{PDB3|1cdu}} :125-203
{{PDB3|2b4c}}C:125–203 {{PDB3|1g9n}}C:125–203 {{PDB3|1cdu}} :125–203
{{PDB3|1rzj}}C:125-203 {{PDB3|1jl4}}D:125-203 {{PDB3|1opw}}C:125-203
{{PDB3|1rzj}}C:125–203 {{PDB3|1jl4}}D:125–203 {{PDB3|1opw}}C:125–203
{{PDB3|1cdy}} :125-203 {{PDB3|1cdj}} :125-203 {{PDB3|3cd4}} :125-203
{{PDB3|1cdy}} :125–203 {{PDB3|1cdj}} :125–203 {{PDB3|3cd4}} :125–203
{{PDB3|1opt}}C:125-203 {{PDB3|1cdh}} :125-203 {{PDB3|1g9m}}C:125-203
{{PDB3|1opt}}C:125–203 {{PDB3|1cdh}} :125–203 {{PDB3|1g9m}}C:125–203
{{PDB3|1opn}}C:125-203 {{PDB3|1vca}}A:133-221 {{PDB3|1ij9}}A:133-220
{{PDB3|1opn}}C:125–203 {{PDB3|1vca}}A:133–221 {{PDB3|1ij9}}A:133–220
{{PDB3|1vsc}}A:133-219
{{PDB3|1vsc}}A:133–219
}}
}}


The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulphide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha, delta, epsilon, gamma and mu, all consisting of a variable domain (VH) and three (in alpha, delta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins, in which the variable and constant domains have clear, conserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; {{InterPro|IPR013106}}), C1-set (constant-1; {{InterPro|IPR003597}}), C2-set (constant-2; {{InterPro|IPR008424}}) and I-set (intermediate; {{InterPro|IPR013098}})<ref name="PUB00014840">{{cite journal |author=Smith DK, Xue H |title=Sequence profiles of immunoglobulin and immunoglobulin-like domains |journal=J. Mol. Biol. |volume=274 |issue=4 |pages=530–545 |year=1997 |pmid=9417933}}</ref>. Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure, with the types differing in the number of strands in the beta-sheets as well as in their sequence patterns<ref name="PUB00015110">{{cite journal |author=Potapov V, Sobolev V, Edelman M, Kister A, Gelfand I |title=Protein-Protein Recognition: Juxtaposition of Domain and Interface Cores in Immunoglobulins and Other Sandwich-like Proteins |journal=J. Mol. Biol. |volume=342 |issue=2 |pages=665–679 |year=2004 |pmid=15327963}}</ref><ref name="PUB00010610">{{cite journal |author=Clarke J, Fowler SB |title=Mapping the folding pathway of an immunoglobulin domain: structural detail from Phi value analysis and movement of the transition state |journal=Structure |volume=9 |issue=5 |pages=355–366 |year=2001 |pmid=11377196}}</ref>.
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulphide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha, delta, epsilon, gamma and mu, all consisting of a variable domain (VH) and three (in alpha, delta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins, in which the variable and constant domains have clear, conserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; {{InterPro|IPR013106}}), C1-set (constant-1; {{InterPro|IPR003597}}), C2-set (constant-2; {{InterPro|IPR008424}}) and I-set (intermediate; {{InterPro|IPR013098}}).<ref name="PUB00014840">{{cite journal |vauthors=Smith DK, Xue H |title=Sequence profiles of immunoglobulin and immunoglobulin-like domains |journal=J. Mol. Biol. |volume=274 |issue=4 |pages=530–545 |year=1997 |pmid=9417933 |doi=10.1006/jmbi.1997.1432}}</ref> Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure, with the types differing in the number of strands in the beta-sheets as well as in their sequence patterns.<ref name="PUB00015110">{{cite journal |vauthors=Potapov V, Sobolev V, Edelman M, Kister A, Gelfand I |title=Protein-Protein Recognition: Juxtaposition of Domain and Interface Cores in Immunoglobulins and Other Sandwich-like Proteins |journal=J. Mol. Biol. |volume=342 |issue=2 |pages=665–679 |year=2004 |pmid=15327963 |doi=10.1016/j.jmb.2004.06.072}}</ref><ref name="PUB00010610">{{cite journal |vauthors=Clarke J, Fowler SB |title=Mapping the folding pathway of an immunoglobulin domain: structural detail from Phi value analysis and movement of the transition state |journal=Structure |volume=9 |issue=5 |pages=355–366 |year=2001 |pmid=11377196 |doi=10.1016/S0969-2126(01)00596-2|doi-access=free }}</ref>


Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein
Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein
families. Ig-like domains are involved in a variety of functions, including cell-cell recognition, cell-surface receptors, muscle structure and the immune system<ref name="PUB00027656">{{cite journal |author=Chothia C, Teichmann SA
families. Ig-like domains are involved in a variety of functions, including [[cell–cell recognition]], cell-surface receptors, muscle structure and the immune system.<ref name="PUB00027656">{{cite journal |vauthors=Chothia C, Teichmann SA |title=Immunoglobulin superfamily proteins in Caenorhabditis elegans |journal=J. Mol. Biol. |volume=296 |issue=5 |pages= 1367–83|year=2000 |pmid=10698639 |doi=10.1006/jmbi.1999.3497|citeseerx=10.1.1.327.6917 }}</ref>
|title=Immunoglobulin superfamily proteins in Caenorhabditis elegans |journal=J. Mol. Biol. |volume=296 |issue=5 |pages=- |year=2000 |pmid=10698639}}</ref>.


'''C2-set domains''', which are Ig-like domains resembling the antibody constant domain. C2-set domains are found primarily in the mammalian T-cell surface antigens CD2 (Cluster of Differentiation 2), CD4 and CD80, as well as in vascular (VCAM) and intercellular (ICAM) cell adhesion molecules.
'''C2-set domains''', which are Ig-like domains resembling the antibody constant domain. C2-set domains are found primarily in the mammalian T-cell surface antigens CD2 (Cluster of Differentiation 2), CD4 and CD80, as well as in vascular (VCAM) and intercellular (ICAM) cell adhesion molecules.


CD2 mediates T-cell adhesion via its ectodomain, and signal transduction utilising its 117-amino acid cytoplasmic tail<ref name="PUB00011269">{{cite journal |author=Reinherz EL, Yang H |title=Dynamic recruitment of human CD2 into lipid rafts. Linkage to T cell signal transduction |journal=J. Biol. Chem. |volume=276 |issue=22 |pages=18775–18785 |year=2001 |pmid=11376005}}</ref>. CD2 displays structural and functional similarities with ''[[African swine fever virus]]'' (ASFV) LMW8-DR, a protein that is involved in cell-cell adhesion and immune response modulation, suggesting
CD2 mediates T-cell adhesion via its ectodomain, and signal transduction utilising its 117-amino acid cytoplasmic tail.<ref name="PUB00011269">{{cite journal |vauthors=Reinherz EL, Yang H |title=Dynamic recruitment of human CD2 into lipid rafts. Linkage to T cell signal transduction |journal=J. Biol. Chem. |volume=276 |issue=22 |pages=18775–18785 |year=2001 |pmid=11376005 | doi=10.1074/jbc.M009852200|doi-access=free }}</ref> CD2 displays structural and functional similarities with ''[[African swine fever virus]]'' (ASFV) LMW8-DR, a protein that is involved in cell–cell adhesion and immune response modulation, suggesting
⚫
a possible role in the pathogenesis of ASFV infection.<ref name="PUB00011270">{{cite journal |vauthors=Kutish GF, Rock DL, Afonso CL, Borca MV, Irusta P, Carrillo C, Brun A, Sussman M |title=An African swine fever virus gene with similarity to the T-lymphocyte surface antigen CD2 mediates hemadsorption |journal=Virology |volume=199 |issue=2 |pages=463–468 |year=1994 |pmid=7907198 |doi=10.1006/viro.1994.1146}}</ref> CD4 is the primary receptor for HIV-1. CD4 has four immunoglobulin-like domains in its extracellular region that share the same structure, but can differ in sequence. Certain extracellular domains may be involved in dimerisation.<ref name="PUB00027654">{{cite journal |author=Sanejouand YH |title=Domain swapping of CD4 upon dimerization |journal=Proteins |volume=57 |issue=1 |pages= 205–12|year=2004 |pmid=15326605 |doi=10.1002/prot.20197}}</ref>
a possible role in the pathogenesis of ASFV infection<ref name="PUB00011270">{{cite journal |author=Kutish GF, Rock

⚫
DL, Afonso CL, Borca MV, Irusta P, Carrillo C, Brun A, Sussman M |title=An African swine fever virus gene with similarity to the T-lymphocyte surface antigen CD2 mediates hemadsorption |journal=Virology |volume=199 |issue=2 |pages=463–468 |year=1994 |pmid=7907198}}</ref>. CD4 is the primary receptor for HIV-1. CD4 has four immunoglobulin-like domains in its extracellular region that share the same structure, but can differ in sequence. Certain extracellular domains may be involved in dimerisation<ref name="PUB00027654">{{cite journal |author=Sanejouand YH |title=Domain swapping of CD4 upon dimerization |journal=Proteins |volume=57 |issue=1 |pages=- |year=2004 |pmid=15326605}}</ref>.
⚫
==Human proteins containing this domain ==
* [[CD2]]
* [[CD4]]
* [[VCAM1]]


==References==
==References==
{{reflist}}
{{reflist}}


⚫
{{InterPro content|IPR008424}}
⚫
==Human proteins containing this domain ==
[[CD2]]; [[CD4]]; [[VCAM1]];

==References==


{{DEFAULTSORT:Immunoglobulin C2-Set Domain}}
[[Category:Protein domains]]
[[Category:Protein domains]]
[[Category:Single-pass transmembrane proteins]]
[[Category:Single-pass transmembrane proteins]]
{{membrane-protein-stub}}


⚫
{{InterPro content|IPR008424}}

Latest revision as of 15:50, 5 July 2021

Immunoglobulin C2-set domain
Identifiers
SymbolC2-set
PfamPF05790
InterProIPR008424
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1wipA:317–388 1wiqB:317–388 1wioB:317–388

1cid :316–386 1hngB:128–198 1hnf :135–205 1rzkC:125–203 1gc1C:125–203 1cdi :125–203 2b4cC:125–203 1g9nC:125–203 1cdu :125–203 1rzjC:125–203 1jl4D:125–203 1opwC:125–203 1cdy :125–203 1cdj :125–203 3cd4 :125–203 1optC:125–203 1cdh :125–203 1g9mC:125–203 1opnC:125–203 1vcaA:133–221 1ij9A:133–220

1vscA:133–219

The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulphide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha, delta, epsilon, gamma and mu, all consisting of a variable domain (VH) and three (in alpha, delta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins, in which the variable and constant domains have clear, conserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; InterPro: IPR013106), C1-set (constant-1; InterPro: IPR003597), C2-set (constant-2; InterPro: IPR008424) and I-set (intermediate; InterPro: IPR013098).[1] Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure, with the types differing in the number of strands in the beta-sheets as well as in their sequence patterns.[2][3]

Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions, including cell–cell recognition, cell-surface receptors, muscle structure and the immune system.[4]

C2-set domains, which are Ig-like domains resembling the antibody constant domain. C2-set domains are found primarily in the mammalian T-cell surface antigens CD2 (Cluster of Differentiation 2), CD4 and CD80, as well as in vascular (VCAM) and intercellular (ICAM) cell adhesion molecules.

CD2 mediates T-cell adhesion via its ectodomain, and signal transduction utilising its 117-amino acid cytoplasmic tail.[5] CD2 displays structural and functional similarities with African swine fever virus (ASFV) LMW8-DR, a protein that is involved in cell–cell adhesion and immune response modulation, suggesting a possible role in the pathogenesis of ASFV infection.[6] CD4 is the primary receptor for HIV-1. CD4 has four immunoglobulin-like domains in its extracellular region that share the same structure, but can differ in sequence. Certain extracellular domains may be involved in dimerisation.[7]

Human proteins containing this domain

[edit]

References

[edit]
  1. ^ Smith DK, Xue H (1997). "Sequence profiles of immunoglobulin and immunoglobulin-like domains". J. Mol. Biol. 274 (4): 530–545. doi:10.1006/jmbi.1997.1432. PMID 9417933.
  2. ^ Potapov V, Sobolev V, Edelman M, Kister A, Gelfand I (2004). "Protein-Protein Recognition: Juxtaposition of Domain and Interface Cores in Immunoglobulins and Other Sandwich-like Proteins". J. Mol. Biol. 342 (2): 665–679. doi:10.1016/j.jmb.2004.06.072. PMID 15327963.
  3. ^ Clarke J, Fowler SB (2001). "Mapping the folding pathway of an immunoglobulin domain: structural detail from Phi value analysis and movement of the transition state". Structure. 9 (5): 355–366. doi:10.1016/S0969-2126(01)00596-2. PMID 11377196.
  4. ^ Chothia C, Teichmann SA (2000). "Immunoglobulin superfamily proteins in Caenorhabditis elegans". J. Mol. Biol. 296 (5): 1367–83. CiteSeerX 10.1.1.327.6917. doi:10.1006/jmbi.1999.3497. PMID 10698639.
  5. ^ Reinherz EL, Yang H (2001). "Dynamic recruitment of human CD2 into lipid rafts. Linkage to T cell signal transduction". J. Biol. Chem. 276 (22): 18775–18785. doi:10.1074/jbc.M009852200. PMID 11376005.
  6. ^ Kutish GF, Rock DL, Afonso CL, Borca MV, Irusta P, Carrillo C, Brun A, Sussman M (1994). "An African swine fever virus gene with similarity to the T-lymphocyte surface antigen CD2 mediates hemadsorption". Virology. 199 (2): 463–468. doi:10.1006/viro.1994.1146. PMID 7907198.
  7. ^ Sanejouand YH (2004). "Domain swapping of CD4 upon dimerization". Proteins. 57 (1): 205–12. doi:10.1002/prot.20197. PMID 15326605.
This article incorporates text from the public domain Pfam and InterPro: IPR008424
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