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| [[Image:1usv.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1usv| PDB=1usv | SCENE= }} | | {{STRUCTURE_1usv| PDB=1usv | SCENE= }} |
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| '''THE STRUCTURE OF THE COMPLEX BETWEEN AHA1 AND HSP90'''
| | ===THE STRUCTURE OF THE COMPLEX BETWEEN AHA1 AND HSP90=== |
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| ==Overview==
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| Hsp90 is a molecular chaperone essential for the activation and assembly of many key eukaryotic signalling and regulatory proteins. Hsp90 is assisted and regulated by co-chaperones that participate in an ordered series of dynamic multiprotein complexes, linked to Hsp90 conformationally coupled ATPase cycle. The co-chaperones Aha1 and Hch1 bind to Hsp90 and stimulate its ATPase activity. Biochemical analysis shows that this activity is dependent on the N-terminal domain of Aha1, which interacts with the central segment of Hsp90. The structural basis for this interaction is revealed by the crystal structure of the N-terminal domain (1-153) of Aha1 (equivalent to the whole of Hch1) in complex with the middle segment of Hsp90 (273-530). Structural analysis and mutagenesis show that binding of N-Aha1 promotes a conformational switch in the middle-segment catalytic loop (370-390) of Hsp90 that releases the catalytic Arg 380 and enables its interaction with ATP in the N-terminal nucleotide-binding domain of the chaperone.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15039704}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15039704 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15039704}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Chaperone]] | | [[Category: Chaperone]] |
| [[Category: Hsp90]] | | [[Category: Hsp90]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:38:35 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:01:02 2008'' |