1fap
From Proteopedia
(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...) |
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| - | [[Image:1fap.gif|left|200px]]<br /> | + | [[Image:1fap.gif|left|200px]]<br /><applet load="1fap" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1fap" size=" | + | |
caption="1fap, resolution 2.7Å" /> | caption="1fap, resolution 2.7Å" /> | ||
'''THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-RAPAMYCIN COMPLEX INTERACTING WITH HUMAN FRAP'''<br /> | '''THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-RAPAMYCIN COMPLEX INTERACTING WITH HUMAN FRAP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Rapamycin, a potent immunosuppressive agent, binds two proteins: the | + | 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== | ==About this Structure== | ||
| - | 1FAP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with RAP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http:// | + | 1FAP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=RAP:'>RAP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FAP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Choi, J.]] | [[Category: Choi, J.]] | ||
[[Category: Clardy, J.]] | [[Category: Clardy, J.]] | ||
| - | [[Category: Schreiber, S | + | [[Category: Schreiber, S L.]] |
[[Category: RAP]] | [[Category: RAP]] | ||
[[Category: complex (isomerase/kinase)]] | [[Category: complex (isomerase/kinase)]] | ||
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[[Category: rapamycin]] | [[Category: rapamycin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:36:46 2008'' |
Revision as of 10:36, 21 February 2008
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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 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
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