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1ihg

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[[Image:1ihg.gif|left|200px]]
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{{STRUCTURE_1ihg| PDB=1ihg | SCENE= }}
{{STRUCTURE_1ihg| PDB=1ihg | SCENE= }}
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'''Bovine Cyclophilin 40, monoclinic form'''
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===Bovine Cyclophilin 40, monoclinic form===
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==Overview==
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BACKGROUND: The "large immunophilin" family consists of domains of cyclophilin or FK506 binding protein linked to a tetratricopeptide (TPR) domain. They are intimately associated with steroid receptor complexes and bind to the C-terminal domain of Hsp90 via the TPR domain. The competitive binding of specific large immunophilins and other TPR-Hsp90 proteins provides a regulatory mechanism for Hsp90 chaperone activity. RESULTS: We have solved the X-ray structures of monoclinic and tetragonal forms of Cyp40. In the monoclinic form, the TPR domain consists of seven helices of variable length incorporating three TPR motifs, which provide a convincing binding surface for the Hsp90 C-terminal MEEVD sequence. The C-terminal residues of Cyp40 protrude out beyond the body of the TPR domain to form a charged helix-the putative calmodulin binding site. However, in the tetragonal form, two of the TPR helices have straightened out to form one extended helix, providing a dramatically different conformation of the molecule. CONCLUSIONS: The X-ray structures are consistent with the role of Cyclophilin 40 as a multifunctional signaling protein involved in a variety of protein-protein interactions. The intermolecular helix-helix interactions in the tetragonal form mimic the intramolecular interactions found in the fully folded monoclinic form. These conserved intra- and intermolecular TPR-TPR interactions are illustrative of a high-fidelity recognition mechanism. The two structures also open up the possibility that partially folded forms of TPR may be important in domain swapping and protein recognition.
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(as it appears on PubMed at http://www.pubmed.gov), where 11377203 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11377203}}
==About this Structure==
==About this Structure==
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[[Category: Walkinshaw, M D.]]
[[Category: Walkinshaw, M D.]]
[[Category: Ppiase immunophilin tetratricopeptide]]
[[Category: Ppiase immunophilin tetratricopeptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:00:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 12:11:45 2008''

Revision as of 09:11, 1 July 2008

Template:STRUCTURE 1ihg

Bovine Cyclophilin 40, monoclinic form

Template:ABSTRACT PUBMED 11377203

About this Structure

1IHG is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Two structures of cyclophilin 40: folding and fidelity in the TPR domains., Taylor P, Dornan J, Carrello A, Minchin RF, Ratajczak T, Walkinshaw MD, Structure. 2001 May 9;9(5):431-8. PMID:11377203

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