2bb2: Difference between revisions

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[[Image:2bb2.jpg|left|200px]]
{{Seed}}
[[Image:2bb2.png|left|200px]]


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{{STRUCTURE_2bb2|  PDB=2bb2  |  SCENE=  }}  
{{STRUCTURE_2bb2|  PDB=2bb2  |  SCENE=  }}  


'''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===




==Overview==
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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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{{ABSTRACT_PUBMED_2234050}}


==About this Structure==
==About this Structure==
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[[Category: Slingsby, C.]]
[[Category: Slingsby, C.]]
[[Category: Eye lens protein]]
[[Category: Eye lens protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:03:36 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:16:51 2008''

Revision as of 03:16, 28 July 2008

File:2bb2.png

Template:STRUCTURE 2bb2

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

Template:ABSTRACT PUBMED 2234050

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

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