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{{Cite journal | author=Liu F| title=Galectins: Regulators of acute and chronic inflammation | journal=[[Annals of the New York Academy of Sciences]] | volume=1183 | year=2010 | pages=158-182 | doi=10.1111/j.1749-6632.2009.05131.x.}} |
{{Cite journal | author=Liu F| title=Galectins: Regulators of acute and chronic inflammation | journal=[[Annals of the New York Academy of Sciences]] | volume=1183 | year=2010 | pages=158-182 | doi=10.1111/j.1749-6632.2009.05131.x.}} |
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</ref>. This is concentration dependent. |
</ref>. This is concentration dependent. |
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http://www.ncbi.nlm.nih.gov/books/NBK1944/ |
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{{Reflist}} |
{{Reflist}} |
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Revision as of 14:55, 19 March 2013
GALECTINS
Galectins are soluble proteins without membrane binding domains that are found to have intra- and extracellular functions.
Structure
There are three different forms of galectin structure, dimeric, tandem or chimera. Dimeric galectins, also called prototypical galectins, are homodimers of two identical galectin subunits that have associated with one another. The galectins that fall under this category are galectin-1, -2, -5, -7, -10, -11, -13 and -14. Tandem galectins contained at least two distinct carbohydrate recognition domains within one polypeptide. The CRDs are linked with a small peptide domain. Tandem galectins include galectin-4, -5, -8, -9 and -12. The final galectin is galectin-3 which is the only galectin found in the chimera category in vertebrates. Galectin-3 has one CRD and a long non-lectin domain. Galectin-3 can exist in monomeric form or can associate via the non-lectin domain into multivalent complexes [1]. This is concentration dependent.
http://www.ncbi.nlm.nih.gov/books/NBK1944/
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Liu F (2010). "Galectins: Regulators of acute and chronic inflammation". Annals of the New York Academy of Sciences. 1183: 158–182. doi:10.1111/j.1749-6632.2009.05131.x.
{{cite journal}}: Check|doi=value (help)