1fkf
From Proteopedia
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| - | [[Image:1fkf.gif|left|200px]] | + | [[Image:1fkf.gif|left|200px]] |
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| - | '''ATOMIC STRUCTURE OF FKBP-FK506, AN IMMUNOPHILIN-IMMUNOSUPPRESSANT COMPLEX''' | + | {{Structure |
| + | |PDB= 1fkf |SIZE=350|CAPTION= <scene name='initialview01'>1fkf</scene>, resolution 1.7Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FK5:8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN'>FK5</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ATOMIC STRUCTURE OF FKBP-FK506, AN IMMUNOPHILIN-IMMUNOSUPPRESSANT COMPLEX''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FKF is a [ | + | 1FKF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FKF OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/1709302 1709302] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: isomerase]] | [[Category: isomerase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:10:15 2008'' |
Revision as of 09:10, 20 March 2008
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| 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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