2jdf

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(New page: 200px<br /><applet load="2jdf" size="350" color="white" frame="true" align="right" spinBox="true" caption="2jdf, resolution 1.7&Aring;" /> '''HUMAN GAMMA-B CRYSTAL...)
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[[Image:2jdf.jpg|left|200px]]<br /><applet load="2jdf" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2jdf, resolution 1.7&Aring;" />
 
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'''HUMAN GAMMA-B CRYSTALLIN'''<br />
 
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==Overview==
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==Human gamma-B crystallin==
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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.
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<StructureSection load='2jdf' size='340' side='right'caption='[[2jdf]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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== Disease ==
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[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>
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== Function ==
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[https://www.uniprot.org/uniprot/CRGB_HUMAN CRGB_HUMAN] Crystallins are the dominant structural components of the vertebrate eye lens.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jd/2jdf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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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2JDF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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 Jun 22;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17628592 17628592]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 2jdf" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Ebersbach, H.]]
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[[Category: Fiedler, E.]]
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[[Category: Fiedler, M.]]
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[[Category: Fiedler, U.]]
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[[Category: Proetzel, G.]]
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[[Category: Reimann, C.]]
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[[Category: Rudolph, R.]]
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[[Category: Scheuermann, T.]]
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[[Category: Stubbs, M.T.]]
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[[Category: affilin]]
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[[Category: artificial binding protein]]
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[[Category: eye lens protein]]
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[[Category: gamma crystallin]]
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[[Category: oxidation]]
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[[Category: phosphorylation]]
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[[Category: polymorphism]]
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[[Category: structural protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:49:11 2008''
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==See Also==
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*[[Crystallin 3D structures|Crystallin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Ebersbach H]]
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[[Category: Fiedler E]]
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[[Category: Fiedler M]]
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[[Category: Fiedler U]]
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[[Category: Proetzel G]]
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[[Category: Reimann C]]
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[[Category: Rudolph R]]
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[[Category: Scheuermann T]]
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[[Category: Stubbs MT]]

Current revision

Human gamma-B crystallin

PDB ID 2jdf

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