1bd7

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[[Image:1bd7.png|left|200px]]
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==CIRCULARLY PERMUTED BB2-CRYSTALLIN==
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<StructureSection load='1bd7' size='340' side='right' caption='[[1bd7]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1bd7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BD7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BD7 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bd7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bd7 RCSB], [http://www.ebi.ac.uk/pdbsum/1bd7 PDBsum]</span></td></tr>
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<table>
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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/bd/1bd7_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/chain_selection.php?pdb_ID=2ata 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 betagamma-crystallins form a superfamily of eye lens proteins comprised of multiple Greek motifs that are symmetrically organized into domains and higher assemblies. In the betaB2-crystallin dimer each polypeptide folds into two similar domains that are related to monomeric gamma-crystallin by domain swapping. The crystal structure of the circularly permuted two-domain betaB2 polypeptide shows that permutation converts intermolecular domain pairing into intramolecular pairing. However, the dimeric permuted protein is, in fact, half a native tetramer. This result shows how the sequential order of domains in multi-domain proteins can affect quaternary domain assembly.
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{{STRUCTURE_1bd7| PDB=1bd7 | SCENE= }}
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Circular permutation of betaB2-crystallin changes the hierarchy of domain assembly.,Wright G, Basak AK, Wieligmann K, Mayr EM, Slingsby C Protein Sci. 1998 Jun;7(6):1280-5. PMID:9655330<ref>PMID:9655330</ref>
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===CIRCULARLY PERMUTED BB2-CRYSTALLIN===
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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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{{ABSTRACT_PUBMED_9655330}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1bd7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BD7 OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:009655330</ref><references group="xtra"/>
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Basak, A K.]]
[[Category: Basak, A K.]]

Revision as of 03:14, 7 August 2014

CIRCULARLY PERMUTED BB2-CRYSTALLIN

1bd7, resolution 2.78Å

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