1fkf: Difference between revisions

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

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

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~~'''~~ATOMIC STRUCTURE OF FKBP-FK506, AN IMMUNOPHILIN-IMMUNOSUPPRESSANT COMPLEX~~'''~~

===ATOMIC STRUCTURE OF FKBP-FK506, AN IMMUNOPHILIN-IMMUNOSUPPRESSANT COMPLEX===

~~==Overview==~~

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The ~~structure of the human FK506 binding protein (FKBP)~~, ~~complexed with~~ the ~~immunosuppressant FK506, has been determined~~ to 1.~~7 angstroms resolution by x-ray crystallography~~. ~~The conformation of the protein changes little upon complexation~~, ~~but the conformation of FK506~~ is ~~markedly different in~~ the bound and unbound forms. The drug's association with the protein involves five hydrogen bonds, a hydrophobic binding pocket lined with conserved aromatic residues, and an unusual carbonyl binding pocket. The nature of this complex has implications for the mechanism of rotamase catalysis and for the biological actions of FK506 and rapamycin.

The line below this paragraph, {{ABSTRACT_PUBMED_1709302}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 1709302 is the PubMed ID number.

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==About this Structure==

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[[Category: Vanduyne, G D.]]

[[Category: Isomerase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 16~~:25:48 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:23:58 2008''

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-[[Image:1fkf.gif|left|200px]]
+{{Seed}}
+[[Image:1fkf.png|left|200px]]
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 {{STRUCTURE_1fkf|  PDB=1fkf  |  SCENE=  }}
-'''ATOMIC STRUCTURE OF FKBP-FK506, AN IMMUNOPHILIN-IMMUNOSUPPRESSANT COMPLEX'''
+===ATOMIC STRUCTURE OF FKBP-FK506, AN IMMUNOPHILIN-IMMUNOSUPPRESSANT COMPLEX===
-==Overview==
+<!--
-The structure of the human FK506 binding protein (FKBP), complexed with the immunosuppressant FK506, has been determined to 1.7 angstroms resolution by x-ray crystallography. The conformation of the protein changes little upon complexation, but the conformation of FK506 is markedly different in the bound and unbound forms. The drug's association with the protein involves five hydrogen bonds, a hydrophobic binding pocket lined with conserved aromatic residues, and an unusual carbonyl binding pocket. The nature of this complex has implications for the mechanism of rotamase catalysis and for the biological actions of FK506 and rapamycin.
+The line below this paragraph, {{ABSTRACT_PUBMED_1709302}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 1709302 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_1709302}}
 ==About this Structure==
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 [[Category: Vanduyne, G D.]]
 [[Category: Isomerase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:25:48 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 03:23:58 2008''