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Chaperone-Assisted RNA Crystallography (CARC)
Chaperone-Assisted RNA Crystallography (CARC) is a method of RNA Crystallography that utilizes a binding protein (chaperone) to facilitate crystal formation. Chaperones include antibodies[1], DARPins[2], and other types of proteins.
Purpose of a chaperone
While crystallography is a popular method for determining the structures of biological molecules [3] (see the PDB's website on number of structures obtained by experimental method here), less than 1,500 of the approximately 130,600 structures in the Protein data bank are of RNA. RNA is negatively charged and has extensive secondary but not tertiary structure, thus RNA does not form appropriate crystal contacts to make a lattice structure. While adding ions help to stabilize the negatively charged backbone, the issue still remains of locking RNA into one rigid conformation so that crystals form and phasing is good.
To combat this problem, chaperones are used to help stabilize RNA and form a regular lattice structure. Common chaperones used in research are Fabs, the region of an antibody that binds the antigen (in this case, RNA), including the paratope.
Applications
Notes
- ^ Sherman, Eileen; Archer, Jennifer; Ye, Jing-Dong (2016). "Fab Chaperone-Assisted RNA Crystallography (Fab CARC)". Methods Molecular Biology. 1320: 77–109. doi:10.1007/978-1-4939-2763-0_7. PMID 26227039.
- ^ Sennhauser, Gaby; Grutter, Markus (October 8, 2008). "Chaperone-Assisted Crystallography with DARPins". Cell Structure. 16 (10): 1443–1453. doi:10.1016/j.str.2008.08.010.
- ^ RCSB Protein Data Bank Statistics