1fap: Difference between revisions

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[[Image:1fap.~~gif~~|left|200px]]

[[Image:1fap.png|left|200px]]

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~~'''~~THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-RAPAMYCIN COMPLEX INTERACTING WITH HUMAN FRAP~~'''~~

===THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-RAPAMYCIN COMPLEX INTERACTING WITH HUMAN FRAP===

~~==Overview==~~

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~~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.

The line below this paragraph, {{ABSTRACT_PUBMED_8662507}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 8662507 is the PubMed ID number.

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==About this Structure==

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[[Category: Frap]]

[[Category: Rapamycin]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 16~~:06:30 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:57:56 2008''

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-[[Image:1fap.gif|left|200px]]
+{{Seed}}
+[[Image:1fap.png|left|200px]]
 <!--
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 {{STRUCTURE_1fap|  PDB=1fap  |  SCENE=  }}
-'''THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-RAPAMYCIN COMPLEX INTERACTING WITH HUMAN FRAP'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_8662507}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8662507 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8662507}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Frap]]
 [[Category: Rapamycin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:06:30 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 02:57:56 2008''