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1qsd

From Proteopedia

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[[Image:1qsd.gif|left|200px]]
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{{STRUCTURE_1qsd| PDB=1qsd | SCENE= }}
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'''RBL2P, BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR'''
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===RBL2P, BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10542094 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10542094}}
==About this Structure==
==About this Structure==
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[[Category: Chaperone]]
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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 Tue Jul 29 07:28:46 2008''

Revision as of 04:28, 29 July 2008

Image:1qsd.png

Template:STRUCTURE 1qsd

RBL2P, BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR

Template:ABSTRACT PUBMED 10542094

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 Tue Jul 29 07:28:46 2008

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