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PDBsum entry 1c9h
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Immune system
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PDB id
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1c9h
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of fkbp12.6 in complex with rapamycin.
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Authors
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C.C.Deivanayagam,
M.Carson,
A.Thotakura,
S.V.Narayana,
R.S.Chodavarapu.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2000,
56,
266-271.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 3.
Figure 3 Stereo diagrams of the protein surfaces of rapamycin
complexes of FKBP12.6 and FKBP12. The rapamycin is shown in
ball-and-stick format, colored white, red and blue for carbon,
oxygen and nitrogen, respectively. The protein surfaces are
colored by chemical property: white is hydrophobic, red is
negatively charged, blue is positively charged, orange is a
hydrogen-bond acceptor, cyan is a hydrogen-bond donor and
magenta can both accept and donate hydrogen bonds. Exposed
surfaces of non-identical residues are textured with a mesh and
labeled. The orientation is as in Fig. 1-(b), only 90% smaller.
Above, FKBP12.6; below, FKBP12.
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Figure 4.
Figure 4 Stereo diagrams of the hydrophobic binding pockets of
FKBP12.6 and FKBP12. All residues and surfaces within 4 Å of
rapamycin are shown. Ribbons and carbon are white in FKBP12.6
and gray in FKBP12. O atoms and N atoms are red and blue,
respectively, in both. Hydrogen bonds are shown as dashed black
lines.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2000,
56,
266-271)
copyright 2000.
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