2jdg

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[[Image:2jdg.jpg|left|200px]]
 
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{{Structure
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==Affilin based on HUMAN GAMMA-B CRYSTALLIN==
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|PDB= 2jdg |SIZE=350|CAPTION= <scene name='initialview01'>2jdg</scene>, resolution 2.0&Aring;
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<StructureSection load='2jdg' size='340' side='right'caption='[[2jdg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[2jdg]] 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=2JDG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JDG FirstGlance]. <br>
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|ACTIVITY=
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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]] 2&#8491;</td></tr>
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|GENE=
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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=2jdg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jdg OCA], [https://pdbe.org/2jdg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jdg RCSB], [https://www.ebi.ac.uk/pdbsum/2jdg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jdg ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1leu|1LEU]], [[1myv|1MYV]], [[1myx|1MYX]], [[1myy|1MYY]], [[1mz1|1MZ1]], [[1mz2|1MZ2]], [[1mz3|1MZ3]], [[2jdf|2JDF]]
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== Disease ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jdg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jdg OCA], [http://www.ebi.ac.uk/pdbsum/2jdg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2jdg RCSB]</span>
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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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}}
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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/2jdg_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=2jdg 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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'''AFFILIN BASED ON HUMAN GAMMA-B CRYSTALLIN'''
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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2jdg" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Crystallin 3D structures|Crystallin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2JDG is a [[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=2JDG OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17628592 17628592]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Ebersbach, H.]]
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[[Category: Ebersbach H]]
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[[Category: Fiedler, E.]]
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[[Category: Fiedler E]]
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[[Category: Fiedler, M.]]
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[[Category: Fiedler M]]
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[[Category: Fiedler, U.]]
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[[Category: Fiedler U]]
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[[Category: Proetzel, G.]]
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[[Category: Proetzel G]]
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[[Category: Reimann, C.]]
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[[Category: Reimann C]]
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[[Category: Rudolph, R.]]
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[[Category: Rudolph R]]
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[[Category: Scheuermann, T.]]
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[[Category: Scheuermann T]]
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[[Category: Stubbs, M T.]]
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[[Category: Stubbs MT]]
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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 Mon Mar 31 03:56:38 2008''
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Current revision

Affilin based on HUMAN GAMMA-B CRYSTALLIN

PDB ID 2jdg

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