2jdf: Difference between revisions

New page: left|200px<br /><applet load="2jdf" size="350" color="white" frame="true" align="right" spinBox="true" caption="2jdf, resolution 1.7Å" /> '''HUMAN GAMMA-B CRYSTAL...
 
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'''HUMAN GAMMA-B CRYSTALLIN'''<br />


==Overview==
==Human gamma-B crystallin==
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.
<StructureSection load='2jdf' size='340' side='right'caption='[[2jdf]], [[Resolution|resolution]] 1.70&Aring;' 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]] 1.7&#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=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.


==About this Structure==
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>
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].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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]
</div>
<div class="pdbe-citations 2jdf" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Crystallin 3D structures|Crystallin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[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]]
 
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