4gr7: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4gr7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GR7 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=4gr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gr7 OCA], [https://pdbe.org/4gr7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gr7 RCSB], [https://www.ebi.ac.uk/pdbsum/4gr7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gr7 ProSAT]</span></td></tr>
 </table>
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 == Function ==
 [https://www.uniprot.org/uniprot/CRGD_HUMAN CRGD_HUMAN] Crystallins are the dominant structural components of the vertebrate eye lens.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Some mutants of human gammaD-crystallin are closely linked to congenital cataracts, although the detailed molecular mechanisms of mutant-associated cataract formation are generally not known. Here we report on a recently discovered gammaD-crystallin mutant (W42R) that has been linked to autosomal dominant, congenital cataracts in a Chinese family. The mutant protein is much less soluble and stable than wild-type gammaD-crystallin. We solved the crystal structure of W42R at 1.7 A resolution, which revealed only minor differences from the wild-type structure. Interestingly, the W42R variant is highly susceptible to protease digestion, suggesting the presence of a small population of partially unfolded protein. This partially unfolded species was confirmed and quantified by NMR spectroscopy. Hydrogen/deuterium exchange experiments revealed chemical exchange between the folded and unfolded species. Exposure of wild-type gammaD-crystallin to UV caused damage to the N-terminal domain of the protein, resulting in very similar proteolytic susceptibility as observed for the W42R mutant. Altogether, our combined data allowed us to propose a model for W42R pathogenesis, with the W42R mutant serving as a mimic for photodamaged gammaD-crystallin involved in age-related cataract.
-The human W42R gammaD-crystallin mutant structure provides a link between congenital and age-related cataracts.,Ji F, Jung J, Koharudin LM, Gronenborn AM J Biol Chem. 2013 Jan 4;288(1):99-109. doi: 10.1074/jbc.M112.416354. Epub 2012, Nov 2. PMID:23124202<ref>PMID:23124202</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4gr7" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>