2jdf
From Proteopedia
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| - | [[Image:2jdf.jpg|left|200px]]<br /><applet load="2jdf" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2jdf, resolution 1.7Å" /> | ||
| - | '''HUMAN GAMMA-B CRYSTALLIN'''<br /> | ||
| - | == | + | ==Human gamma-B crystallin== |
| + | <StructureSection load='2jdf' size='340' side='right'caption='[[2jdf]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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='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> | ||
| + | </table> | ||
| + | == 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> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CRGB_HUMAN CRGB_HUMAN] 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/jd/2jdf_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jdf ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | 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<ref>PMID:17628592</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2jdf" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Crystallin 3D structures|Crystallin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ebersbach H]] | ||
| + | [[Category: Fiedler E]] | ||
| + | [[Category: Fiedler M]] | ||
| + | [[Category: Fiedler U]] | ||
| + | [[Category: Proetzel G]] | ||
| + | [[Category: Reimann C]] | ||
| + | [[Category: Rudolph R]] | ||
| + | [[Category: Scheuermann T]] | ||
| + | [[Category: Stubbs MT]] | ||
Current revision
Human gamma-B crystallin
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Categories: Homo sapiens | Large Structures | Ebersbach H | Fiedler E | Fiedler M | Fiedler U | Proetzel G | Reimann C | Rudolph R | Scheuermann T | Stubbs MT
