1fap
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1fap" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fap, resolution 2.7Å" /> '''THE STRUCTURE OF THE...)
Next diff →
Revision as of 14:44, 12 November 2007
|
THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-RAPAMYCIN COMPLEX INTERACTING WITH HUMAN FRAP
Overview
Rapamycin, a potent immunosuppressive agent, binds two proteins: the, FK506-binding protein (FKBP12) and the FKBP-rapamycin-associated protein, (FRAP). A crystal structure of the ternary complex of human FKBP12, rapamycin, and the FKBP12-rapamycin-binding (FRB) domain of human FRAP at, a resolution of 2.7 angstroms revealed the two proteins bound together as, a result of the ability of rapamycin to occupy two different hydrophobic, binding pockets simultaneously. The structure shows extensive interactions, between rapamycin and both proteins, but fewer interactions between the, proteins. The structure of the FRB domain of FRAP clarifies both, rapamycin-independent and -dependent effects observed for mutants of FRAP, and its homologs in the family of proteins related to the, ataxia-telangiectasia mutant gene product, and it illustrates how a small, cell-permeable molecule can mediate protein dimerization.
About this Structure
1FAP is a Protein complex structure of sequences from Homo sapiens with RAP as ligand. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 Full crystallographic information is available from OCA.
Reference
Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP., Choi J, Chen J, Schreiber SL, Clardy J, Science. 1996 Jul 12;273(5272):239-42. PMID:8662507
Page seeded by OCA on Mon Nov 12 16:50:49 2007
