1us7
From Proteopedia
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| - | [[Image:1us7.jpg|left|200px]] | + | [[Image:1us7.jpg|left|200px]] |
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| - | '''COMPLEX OF HSP90 AND P50''' | + | {{Structure |
| + | |PDB= 1us7 |SIZE=350|CAPTION= <scene name='initialview01'>1us7</scene>, resolution 2.30Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''COMPLEX OF HSP90 AND P50''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1US7 is a [ | + | 1US7 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1US7 OCA]. |
==Reference== | ==Reference== | ||
| - | The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)., Roe SM, Ali MM, Meyer P, Vaughan CK, Panaretou B, Piper PW, Prodromou C, Pearl LH, Cell. 2004 Jan 9;116(1):87-98. PMID:[http:// | + | The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)., Roe SM, Ali MM, Meyer P, Vaughan CK, Panaretou B, Piper PW, Prodromou C, Pearl LH, Cell. 2004 Jan 9;116(1):87-98. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14718169 14718169] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: heat shock]] | [[Category: heat shock]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:36:04 2008'' |
Revision as of 12:36, 20 March 2008
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| , resolution 2.30Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
COMPLEX OF HSP90 AND P50
Overview
Recruitment of protein kinase clients to the Hsp90 chaperone involves the cochaperone p50(cdc37) acting as a scaffold, binding protein kinases via its N-terminal domain and Hsp90 via its C-terminal region. p50(cdc37) also has a regulatory activity, arresting Hsp90's ATPase cycle during client-protein loading. We have localized the binding site for p50(cdc37) to the N-terminal nucleotide binding domain of Hsp90 and determined the crystal structure of the Hsp90-p50(cdc37) core complex. Dimeric p50(cdc37) binds to surfaces of the Hsp90 N-domain implicated in ATP-dependent N-terminal dimerization and association with the middle segment of the chaperone. This interaction fixes the lid segment in an open conformation, inserts an arginine side chain into the ATP binding pocket to disable catalysis, and prevents trans-activating interaction of the N domains.
About this Structure
1US7 is a Protein complex structure of sequences from Homo sapiens and Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)., Roe SM, Ali MM, Meyer P, Vaughan CK, Panaretou B, Piper PW, Prodromou C, Pearl LH, Cell. 2004 Jan 9;116(1):87-98. PMID:14718169
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