2m3t

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2m3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m3t OCA], [https://pdbe.org/2m3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m3t RCSB], [https://www.ebi.ac.uk/pdbsum/2m3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m3t ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Transparency in the eye lens is maintained via specific, functional interactions among the structural betagamma- and chaperone alpha-crystallins. Here, we report the structure and alpha-crystallin binding interface of the G18V variant of human gammaS-crystallin (gammaS-G18V), which is linked to hereditary childhood-onset cortical cataract. Comparison of the solution nuclear magnetic resonance structures of wild-type and G18V gammaS-crystallin, both presented here, reveal that the increased aggregation propensity of gammaS-G18V results from neither global misfolding nor the solvent exposure of a hydrophobic residue but instead involves backbone rearrangement within the N-terminal domain. alphaB-crystallin binds more strongly to the variant, via a well-defined interaction surface observed via chemical shift differences. In the context of the alphaB-crystallin structure and the finding that it forms heterogeneous multimers, our structural studies suggest a potential mechanism for cataract formation via the depletion of the finite alphaB-crystallin population of the lens.

Preferential and Specific Binding of Human alphaB-Crystallin to a Cataract-Related Variant of gammaS-Crystallin.,Kingsley CN, Brubaker WD, Markovic S, Diehl A, Brindley AJ, Oschkinat H, Martin RW Structure. 2013 Oct 30. pii: S0969-2126(13)00368-7. doi:, 10.1016/j.str.2013.09.017. PMID:24183572<ref>PMID:24183572</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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