3fap

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{{STRUCTURE_3fap| PDB=3fap | SCENE= }}
{{STRUCTURE_3fap| PDB=3fap | SCENE= }}
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'''ATOMIC STRUCTURES OF THE RAPAMYCIN ANALOGS IN COMPLEX WITH BOTH HUMAN FKBP12 AND FRB DOMAIN OF FRAP'''
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===ATOMIC STRUCTURES OF THE RAPAMYCIN ANALOGS IN COMPLEX WITH BOTH HUMAN FKBP12 AND FRB DOMAIN OF FRAP===
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==Overview==
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The structure of the FKBP12-rapamycin-FRB ternary complex has now been refined at 2.2 A resolution. The cell-cycle arrest agent rapamycin binds FK506-binding protein (FKBP12) and the FKBP12-rapamycin binding (FRB) domain of FKBP12-rapamycin associated protein (FRAP) simultaneously, and the inhibition of FRAP is responsible for rapamycin's biological activity. The conformation of rapamycin in the ternary complex is very similar to that observed in the FKBP12-rapamycin binary complex, with an r.m.s. difference of only 0.30 A. However, a slight (9 degrees ) rotation repositions the FRB-binding face of rapamycin in the ternary complex. There are extensive rapamycin-protein interactions and relatively few interactions between the two protein partners FKBP12 and FRB, these interactions mainly involving residues in the 40s and 80s loops of FKBP12 and alpha1 and alpha4 of FRB. The high-resolution refinement has revealed the crucial role of several buried waters in the formation of the ternary complex.
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(as it appears on PubMed at http://www.pubmed.gov), where 10089303 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10089303}}
==About this Structure==
==About this Structure==
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[[Category: Gene therapy]]
[[Category: Gene therapy]]
[[Category: Rapamycin]]
[[Category: Rapamycin]]
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Revision as of 21:16, 27 July 2008

Image:3fap.png

Template:STRUCTURE 3fap

ATOMIC STRUCTURES OF THE RAPAMYCIN ANALOGS IN COMPLEX WITH BOTH HUMAN FKBP12 AND FRB DOMAIN OF FRAP

Template:ABSTRACT PUBMED 10089303

About this Structure

3FAP is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Refined structure of the FKBP12-rapamycin-FRB ternary complex at 2.2 A resolution., Liang J, Choi J, Clardy J, Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):736-44. PMID:10089303

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