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| | {{STRUCTURE_1iip| PDB=1iip | SCENE= }} | | {{STRUCTURE_1iip| PDB=1iip | SCENE= }} |
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| - | '''Bovine Cyclophilin 40, Tetragonal Form'''
| + | ===Bovine Cyclophilin 40, Tetragonal 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11377203}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11377203 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11377203}} |
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| | ==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]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:02:53 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 12:16:54 2008'' |
Revision as of 09:16, 1 July 2008
Template:STRUCTURE 1iip
Bovine Cyclophilin 40, Tetragonal Form
Template:ABSTRACT PUBMED 11377203
About this Structure
1IIP 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
Page seeded by OCA on Tue Jul 1 12:16:54 2008
