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| | <StructureSection load='2jdf' size='340' side='right'caption='[[2jdf]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='2jdf' size='340' side='right'caption='[[2jdf]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jdf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JDF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JDF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jdf]] is a 1 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=2JDF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JDF FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1leu|1leu]], [[1myv|1myv]], [[1myx|1myx]], [[1myy|1myy]], [[1mz1|1mz1]], [[1mz2|1mz2]], [[1mz3|1mz3]], [[2jdg|2jdg]]</div></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]] 1.7Å</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=2jdf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jdf OCA], [https://pdbe.org/2jdf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jdf RCSB], [https://www.ebi.ac.uk/pdbsum/2jdf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jdf ProSAT]</span></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=2jdf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jdf OCA], [https://pdbe.org/2jdf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jdf RCSB], [https://www.ebi.ac.uk/pdbsum/2jdf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jdf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[https://www.uniprot.org/uniprot/CRGB_HUMAN CRGB_HUMAN]] Zonular cataract;Anterior polar cataract;Total congenital cataract. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:23288985</ref>
| + | [https://www.uniprot.org/uniprot/CRGB_HUMAN CRGB_HUMAN] Zonular cataract;Anterior polar cataract;Total congenital cataract. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:23288985</ref> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CRGB_HUMAN CRGB_HUMAN]] Crystallins are the dominant structural components of the vertebrate eye lens.
| + | [https://www.uniprot.org/uniprot/CRGB_HUMAN CRGB_HUMAN] Crystallins are the dominant structural components of the vertebrate eye lens. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ebersbach, H]] | + | [[Category: Ebersbach H]] |
| - | [[Category: Fiedler, E]] | + | [[Category: Fiedler E]] |
| - | [[Category: Fiedler, M]] | + | [[Category: Fiedler M]] |
| - | [[Category: Fiedler, U]] | + | [[Category: Fiedler U]] |
| - | [[Category: Proetzel, G]] | + | [[Category: Proetzel G]] |
| - | [[Category: Reimann, C]] | + | [[Category: Reimann C]] |
| - | [[Category: Rudolph, R]] | + | [[Category: Rudolph R]] |
| - | [[Category: Scheuermann, T]] | + | [[Category: Scheuermann T]] |
| - | [[Category: Stubbs, M T]] | + | [[Category: Stubbs MT]] |
| - | [[Category: Affilin]]
| + | |
| - | [[Category: Artificial binding protein]]
| + | |
| - | [[Category: Eye lens protein]]
| + | |
| - | [[Category: Gamma crystallin]]
| + | |
| - | [[Category: Oxidation]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Polymorphism]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Disease
CRGB_HUMAN Zonular cataract;Anterior polar cataract;Total congenital cataract. The disease is caused by mutations affecting the gene represented in this entry.[1]
Function
CRGB_HUMAN 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 concept of novel binding proteins as an alternative to antibodies has undergone rapid development and is now ready for practical use in a wide range of applications. Alternative binding proteins, based on suitable scaffolds with desirable properties, are selected from combinatorial libraries in vitro. Here, we describe an approach using a beta-sheet of human gamma-B-crystallin to generate a universal binding site through randomization of eight solvent-exposed amino acid residues selected according to structural and sequence analyses. Specific variants, so-called Affilin, have been isolated from a phage display library against a variety of targets that differ considerably in size and structure. The isolated Affilin variants can be produced in Escherichia coli as soluble proteins and have a high level of thermodynamic stability. The crystal structures of the human wild-type gamma-B-crystallin and a selected Affilin variant have been determined to 1.7 A and 2.0 A resolution, respectively. Comparison of the two molecules indicates that the human gamma-B-crystallin tolerates amino acid exchanges with no major structural change. We conclude that the intrinsically stable and easily expressed gamma-B-crystallin provides a suitable framework for the generation of novel binding molecules.
Affilin-novel binding molecules based on human gamma-B-crystallin, an all beta-sheet protein.,Ebersbach H, Fiedler E, Scheuermann T, Fiedler M, Stubbs MT, Reimann C, Proetzel G, Rudolph R, Fiedler U J Mol Biol. 2007 Sep 7;372(1):172-85. Epub 2007 Jun 22. PMID:17628592[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ AlFadhli S, Abdelmoaty S, Al-Hajeri A, Behbehani A, Alkuraya F. Novel crystallin gamma B mutations in a Kuwaiti family with autosomal dominant congenital cataracts reveal genetic and clinical heterogeneity. Mol Vis. 2012;18:2931-6. Epub 2012 Dec 9. PMID:23288985
- ↑ Ebersbach H, Fiedler E, Scheuermann T, Fiedler M, Stubbs MT, Reimann C, Proetzel G, Rudolph R, Fiedler U. Affilin-novel binding molecules based on human gamma-B-crystallin, an all beta-sheet protein. J Mol Biol. 2007 Sep 7;372(1):172-85. Epub 2007 Jun 22. PMID:17628592 doi:10.1016/j.jmb.2007.06.045
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