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2v2u

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Structure of Mouse gammaC-crystallin

Structural highlights

2v2u is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CRGC_MOUSE Crystallins are the dominant structural components of the vertebrate eye lens.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The eye lens is packed with soluble crystallin proteins, providing a lifetime of transparency and light refraction. gamma-Crystallins are major components of the dense, high refractive index central regions of the lens and generally have high solubility, high stability and high levels of cysteine residues. Human gammaC belongs to a group of gamma-crystallins with a pair of cysteine residues at positions 78 and 79. Unlike other gamma-crystallins it has relatively low solubility, whereas mouse gammaC, which has the exposed C79 replaced with arginine, and a novel mouse splice variant, gammaCins, are both highly soluble. Furthermore, human gammaC is extremely stable, while the mouse orthologs are less stable. Evolutionary pressure may have favoured stability over solubility for human gammaC and the reverse for the orthologs in the mouse. Mutation of C79 to R79, in human gammaC, greatly increased solubility, however, neither form produced crystals. Remarkably, when the human gammaD R36S crystallization cataract mutation was mimicked in human gammaC-crystallin, the solubility of gammaC was dramatically increased, although it still did not crystallize. The highly soluble mouse gammaC-crystallin did crystallize. Its X-ray structure was solved and used in homology modelling of human gammaC, and its mutants C79R and R36S. The human gammaD R36S mutant was also modelled from human gammaD coordinates. Molecular dynamics simulation of the six molecules in the solution state showed that the human gammaCs differed from gammaDs in domain pairing, behaviour that correlates with interface sequence changes. When the fluctuations of the calculated molecular dipoles, for the six structures, over time were analysed, characteristic patterns for soluble gammaC and gammaD proteins were observed. Individual sequence changes that increase or decrease solubility correlated well with changes in the magnitude and direction of these dipoles. It is suggested that changes in surface residues have allowed adaptation for the differing needs of human and mouse lenses.

Biophysical properties of gammaC-crystallin in human and mouse eye lens: the role of molecular dipoles.,Purkiss AG, Bateman OA, Wyatt K, Wilmarth PA, David LL, Wistow GJ, Slingsby C J Mol Biol. 2007 Sep 7;372(1):205-22. Epub 2007 Jun 26. PMID:17659303^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Purkiss AG, Bateman OA, Wyatt K, Wilmarth PA, David LL, Wistow GJ, Slingsby C. Biophysical properties of gammaC-crystallin in human and mouse eye lens: the role of molecular dipoles. J Mol Biol. 2007 Sep 7;372(1):205-22. Epub 2007 Jun 26. PMID:17659303 doi:http://dx.doi.org/S0022-2836(07)00845-5

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v2u"

@@ Line 1: / Line 1: @@
 ==Structure of Mouse gammaC-crystallin==
-<StructureSection load='2v2u' size='340' side='right' caption='[[2v2u]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='2v2u' size='340' side='right'caption='[[2v2u]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2v2u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V2U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V2U FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2v2u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V2U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V2U FirstGlance]. <br>
-</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=2v2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v2u OCA], [http://pdbe.org/2v2u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v2u RCSB], [http://www.ebi.ac.uk/pdbsum/2v2u PDBsum]</span></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]] 1.9&#8491;</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=2v2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v2u OCA], [https://pdbe.org/2v2u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v2u RCSB], [https://www.ebi.ac.uk/pdbsum/2v2u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v2u ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CRGC_MOUSE CRGC_MOUSE]] Crystallins are the dominant structural components of the vertebrate eye lens.
+[https://www.uniprot.org/uniprot/CRGC_MOUSE CRGC_MOUSE] Crystallins are the dominant structural components of the vertebrate eye lens.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v2/2v2u_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v2/2v2u_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 26: / Line 28: @@
 </div>
 <div class="pdbe-citations 2v2u" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Crystallin 3D structures|Crystallin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: Bateman, O A]]
+[[Category: Mus musculus]]
-[[Category: David, L L]]
+[[Category: Bateman OA]]
-[[Category: Purkiss, A G]]
+[[Category: David LL]]
-[[Category: Slingsby, C]]
+[[Category: Purkiss AG]]
-[[Category: Wistow, G J]]
+[[Category: Slingsby C]]
-[[Category: Wyatt, K]]
+[[Category: Wistow GJ]]
-[[Category: Eye lens protein]]
+[[Category: Wyatt K]]
-[[Category: Structural protein]]

2v2u

From Proteopedia

Current revision

Structure of Mouse gammaC-crystallin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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