1hx1

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{{STRUCTURE_1hx1| PDB=1hx1 | SCENE= }}
{{STRUCTURE_1hx1| PDB=1hx1 | SCENE= }}
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'''CRYSTAL STRUCTURE OF A BAG DOMAIN IN COMPLEX WITH THE HSC70 ATPASE DOMAIN'''
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===CRYSTAL STRUCTURE OF A BAG DOMAIN IN COMPLEX WITH THE HSC70 ATPASE DOMAIN===
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==Overview==
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Bag (Bcl2-associated athanogene) domains occur in a class of cofactors of the eukaryotic chaperone 70-kilodalton heat shock protein (Hsp70) family. Binding of the Bag domain to the Hsp70 adenosine triphosphatase (ATPase) domain promotes adenosine 5'-triphosphate-dependent release of substrate from Hsp70 in vitro. In a 1.9 angstrom crystal structure of a complex with the ATPase of the 70-kilodalton heat shock cognate protein (Hsc70), the Bag domain forms a three-helix bundle, inducing a conformational switch in the ATPase that is incompatible with nucleotide binding. The same switch is observed in the bacterial Hsp70 homolog DnaK upon binding of the structurally unrelated nucleotide exchange factor GrpE. Thus, functional convergence has allowed proteins with different architectures to trigger a conserved conformational shift in Hsp70 that leads to nucleotide exchange.
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(as it appears on PubMed at http://www.pubmed.gov), where 11222862 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11222862}}
==About this Structure==
==About this Structure==
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[[Category: Protein folding]]
[[Category: Protein folding]]
[[Category: Protein-protein complex]]
[[Category: Protein-protein complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:18:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:03:01 2008''

Revision as of 07:03, 1 July 2008

Template:STRUCTURE 1hx1

CRYSTAL STRUCTURE OF A BAG DOMAIN IN COMPLEX WITH THE HSC70 ATPASE DOMAIN

Template:ABSTRACT PUBMED 11222862

About this Structure

1HX1 is a Protein complex structure of sequences from Bos taurus and Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors., Sondermann H, Scheufler C, Schneider C, Hohfeld J, Hartl FU, Moarefi I, Science. 2001 Feb 23;291(5508):1553-7. PMID:11222862

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