1qsd

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[[Image:1qsd.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qsd OCA], [http://www.ebi.ac.uk/pdbsum/1qsd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qsd RCSB]</span>
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'''RBL2P, BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR'''
'''RBL2P, BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Steinbacher, S.]]
[[Category: Steinbacher, S.]]
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[[Category: chaperone]]
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[[Category: Chaperone]]
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[[Category: four-helix-bundle]]
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[[Category: Four-helix-bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:39:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:18:18 2008''
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Revision as of 03:39, 3 May 2008

Image:1qsd.gif

Template:STRUCTURE 1qsd

RBL2P, BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR


Overview

The folding pathway of tubulins includes highly specific interactions with a series of cofactors (A, B, C, D and E) after they are released from the eukaryotic chaperonin CCT. The 2.2 A crystal structure of Rbl2p, the Saccharomyces cerevisiae homolog of beta-tubulin specific cofactor A, shows alpha-helical monomers forming a flat, slightly convex dimer. The surface of the molecule is dominated by polar and charged residues and lacks hydrophobic patches typically observed for chaperones that bind unfolded or partially folded proteins. This post-chaperonin cofactor is therefore clearly distinct from typical chaperones where hydrophobicity is a hallmark of substrate recognition.

About this Structure

1QSD is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Crystal structure of the post-chaperonin beta-tubulin binding cofactor Rbl2p., Steinbacher S, Nat Struct Biol. 1999 Nov;6(11):1029-32. PMID:10542094 Page seeded by OCA on Sat May 3 06:39:03 2008

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