1fkf
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fkf OCA], [http://www.ebi.ac.uk/pdbsum/1fkf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fkf RCSB]</span> | ||
}} | }} | ||
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[[Category: Standaert, R F.]] | [[Category: Standaert, R F.]] | ||
[[Category: Vanduyne, G D.]] | [[Category: Vanduyne, G D.]] | ||
| - | [[Category: FK5]] | ||
[[Category: isomerase]] | [[Category: isomerase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:24:37 2008'' |
Revision as of 17:24, 30 March 2008
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| , resolution 1.7Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
1FKF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex., Van Duyne GD, Standaert RF, Karplus PA, Schreiber SL, Clardy J, Science. 1991 May 10;252(5007):839-42. PMID:1709302
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