2bb2

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[[Image:2bb2.jpg|left|200px]]
[[Image:2bb2.jpg|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_2bb2", creates the "Structure Box" on the page.
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{{STRUCTURE_2bb2| PDB=2bb2 | SCENE= }}
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|RESOURCES=<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.ebi.ac.uk/pdbsum/2bb2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bb2 RCSB]</span>
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'''X-RAY ANALYSIS OF BETA B2-CRYSTALLIN AND EVOLUTION OF OLIGOMERIC LENS PROTEINS'''
'''X-RAY ANALYSIS OF BETA B2-CRYSTALLIN AND EVOLUTION OF OLIGOMERIC LENS PROTEINS'''
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[[Category: Nalini, V.]]
[[Category: Nalini, V.]]
[[Category: Slingsby, C.]]
[[Category: Slingsby, C.]]
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[[Category: eye lens protein]]
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[[Category: Eye lens protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:03:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:03:45 2008''
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Revision as of 17:03, 3 May 2008

Template:STRUCTURE 2bb2

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


Overview

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.

About this Structure

2BB2 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 20:03:36 2008

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