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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5vh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vh1 OCA], [http://pdbe.org/5vh1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vh1 RCSB], [http://www.ebi.ac.uk/pdbsum/5vh1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vh1 ProSAT]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5vh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vh1 OCA], [http://pdbe.org/5vh1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vh1 RCSB], [http://www.ebi.ac.uk/pdbsum/5vh1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vh1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Previous attempts to crystallize mammalian gammaS-crystallin were unsuccessful. Native L16 chicken gammaS crystallized avidly while the Q16 mutant did not. The X-ray structure for chicken gammaS at 2.3 A resolution shows the canonical structure of the superfamily plus a well-ordered N arm aligned with a beta sheet of a neighboring N domain. L16 is also in a lattice contact, partially shielded from solvent. Unexpectedly, the major lattice contact matches a conserved interface (QR) in the multimeric beta-crystallins. QR shows little conservation of residue contacts, except for one between symmetry-related tyrosines, but molecular dipoles for the proteins with QR show striking similarities while other gamma-crystallins differ. In gammaS, QR has few hydrophobic contacts and features a thin layer of tightly bound water. The free energy of QR is slightly repulsive and analytical ultracentrifugation confirms no dimerization in solution. The lattice contacts suggest how gamma-crystallins allow close packing without aggregation in the crowded environment of the lens. | ||
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| + | Crystal Structure of Chicken gammaS-Crystallin Reveals Lattice Contacts with Implications for Function in the Lens and the Evolution of the betagamma-Crystallins.,Sagar V, Chaturvedi SK, Schuck P, Wistow G Structure. 2017 Jul 5;25(7):1068-1078.e2. doi: 10.1016/j.str.2017.05.015. Epub, 2017 Jun 22. PMID:28648607<ref>PMID:28648607</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5vh1" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 17:04, 20 October 2017
Crystal Structure of Chicken Gamma S Crystallin
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