PDBsum entry 1c9h

Immune system

PDB id: 1c9h

Contents

Protein chain

107 a.a. *

Ligands

RAP

Waters ×101

* Residue conservation analysis

PDB id:

1c9h

Name:

Immune system

Title:

Crystal structure of fkbp12.6 in complex with rapamycin

Structure:

Fkbp12.6. Chain: a. Fragment: fkbp12.6. Synonym: calcineurin. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Organ: brain. Gene: cdna. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.00Å R-factor: 0.205 R-free: 0.249

Authors:

C.C.S.Deivanayagam,M.Carson,A.Thotakura,S.V.L.Narayana, C.S.Chodavarapu

Key ref:

C.C.Deivanayagam et al. (2000). Structure of FKBP12.6 in complex with rapamycin. Acta Crystallogr D Biol Crystallogr, 56, 266-271. PubMed id: 10713512 DOI: 10.1107/S0907444999016571

Date:

02-Aug-99 Release date: 03-Aug-00

Protein chain

P68106  (FKB1B_HUMAN) -  Peptidyl-prolyl cis-trans isomerase FKBP1B from Homo sapiens

Seq: 108 a.a.

Struc: 107 a.a.

Enzyme reactions

• Enzyme class: E.C.5.2.1.8 - peptidylprolyl isomerase.
• Reaction: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1107/S0907444999016571

Acta Crystallogr D Biol Crystallogr 56:266-271 (2000)

PubMed id: 10713512

Structure of FKBP12.6 in complex with rapamycin.

C.C.Deivanayagam, M.Carson, A.Thotakura, S.V.Narayana, R.S.Chodavarapu.

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.

Selected figure(s)

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.

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.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2000, 56, 266-271) copyright 2000.

Figures were selected by an automated process.