1C9H

CRYSTAL STRUCTURE OF FKBP12.6 IN COMPLEX WITH RAPAMYCIN

Summary for 1C9H

• Entry DOI: 10.2210/pdb1c9h/pdb
• Related: 1FAP 1FKL
• Descriptor: FKBP12.6, RAPAMYCIN IMMUNOSUPPRESSANT DRUG (3 entities in total)
• Functional Keywords: fkbp12, rapamycin, complex, ryanodine receptor, immune system
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 12581.48

Authors

Deivanayagam, C.C.S.,Carson, M.,Thotakura, A.,Narayana, S.V.L.,Chodavarapu, C.S. (deposition date: 1999-08-02, release date: 2000-08-03, Last modification date: 2024-02-07)

Primary citation

Deivanayagam, C.C.,Carson, M.,Thotakura, A.,Narayana, S.V.,Chodavarapu, R.S.
Structure of FKBP12.6 in complex with rapamycin.
Acta Crystallogr.,Sect.D, 56:266-271, 2000

PubMed Abstract: FKBP12.6 is a novel isoform of FKBP12, which selectively binds to the cardiac ryanodine receptor (RyR2). The crystal structure of FKBP12.6 in complex with rapamycin has now been determined at 2.0 A resolution. The structures of FKBP12.6 and FKBP12 are nearly identical, except for a displacement observed in the helical region of FKBP12.6 toward the hydrophobic pocket. This displacement was not predicted by homology modeling studies. Analyses of the residues that are likely to confer the RyR2-binding specificity are presented.

PubMed: 10713512
DOI: 10.1107/S0907444999016571

Experimental method

X-RAY DIFFRACTION (2 Å)