2bb2

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[[Image:2bb2.png|left|200px]]
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==X-RAY ANALYSIS OF BETA B2-CRYSTALLIN AND EVOLUTION OF OLIGOMERIC LENS PROTEINS==
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<StructureSection load='2bb2' size='340' side='right' caption='[[2bb2]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2bb2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BB2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BB2 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene><br>
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<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=2bb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bb2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bb2 RCSB], [http://www.ebi.ac.uk/pdbsum/2bb2 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/bb/2bb2_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 beta, gamma-crystallins form a class of homologous proteins in the eye lens. Each gamma-crystallin comprises four topologically equivalent, Greek key motifs; pairs of motifs are organized around a local dyad to give domains and two similar domains are in turn related by a further local dyad. Sequence comparisons and model building predicted that hetero-oligomeric beta-crystallins also had internally quadruplicated subunits, but with extensions at the N and C termini, indicating that beta, gamma-crystallins evolved in two duplication steps from an ancestral protein folded as a Greek key. We report here the X-ray analysis at 2.1 A resolution of beta B2-crystallin homodimer which shows that the connecting peptide is extended and the two domains separated in a way quite unlike gamma-crystallin. Domain interactions analogous to those within monomeric gamma-crystallin are intermolecular and related by a crystallographic dyad in the beta B2-crystallin dimer. This shows how oligomers can evolve by conserving an interface rather than connectivity. A further interaction between dimers suggests a model for more complex aggregates of beta-crystallin in the lens.
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{{STRUCTURE_2bb2| PDB=2bb2 | SCENE= }}
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X-ray analysis of beta B2-crystallin and evolution of oligomeric lens proteins.,Bax B, Lapatto R, Nalini V, Driessen H, Lindley PF, Mahadevan D, Blundell TL, Slingsby C Nature. 1990 Oct 25;347(6295):776-80. PMID:2234050<ref>PMID:2234050</ref>
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===X-RAY ANALYSIS OF BETA B2-CRYSTALLIN AND EVOLUTION OF OLIGOMERIC LENS PROTEINS===
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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_2234050}}
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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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[[2bb2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BB2 OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:002234050</ref><references group="xtra"/>
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Bax, B.]]
[[Category: Bax, B.]]

Revision as of 01:42, 30 September 2014

X-RAY ANALYSIS OF BETA B2-CRYSTALLIN AND EVOLUTION OF OLIGOMERIC LENS PROTEINS

2bb2, resolution 2.10Å

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