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PDBsum entry 1c5f
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Isomerase/immunosuppressant
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PDB id
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1c5f
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Contents |
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(+ 2 more)
177 a.a.
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(+ 2 more)
11 a.a.
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* Residue conservation analysis
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PDB id:
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Isomerase/immunosuppressant
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Title:
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Crystal structure of the cyclophilin-like domain from brugia malayi complexed with cyclosporin a
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Structure:
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Peptidyl-prolyl cis-trans isomerase 1. Chain: a, c, e, g, i, k, m, o. Fragment: cyclophilin-like domain, residues 1-177. Synonym: ppiase 1, rotamase, cyclophilin. Engineered: yes. Cyclosporin a. Chain: b, d, f, h, j, l, n, p. Synonym: cyclosporine, ciclosporin, ciclosporine. Engineered: yes
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Source:
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Brugia malayi. Organism_taxid: 6279. Atcc: 75593. Gene: bmcyp-1. Expressed in: escherichia coli. Expression_system_taxid: 562. Ampr). Synthetic: yes. Tolypocladium inflatum.
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Biol. unit:
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Tetramer (from
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Resolution:
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2.47Å
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R-factor:
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0.201
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R-free:
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0.249
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Authors:
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P.J.Ellis,C.K.S.Carlow,D.Ma,P.Kuhn
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Key ref:
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P.J.Ellis
et al.
(2000).
Crystal structure of the complex of brugia malayi cyclophilin and cyclosporin A.
Biochemistry,
39,
592-598.
PubMed id:
DOI:
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Date:
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22-Nov-99
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Release date:
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03-Dec-99
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Supersedes:
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PROCHECK
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Headers
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References
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Enzyme class:
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Chains A, C, E, G, I, K, M, O:
E.C.5.2.1.8
- peptidylprolyl isomerase.
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Reaction:
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[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
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Peptidylproline (omega=180)
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=
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peptidylproline (omega=0)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Biochemistry
39:592-598
(2000)
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PubMed id:
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Crystal structure of the complex of brugia malayi cyclophilin and cyclosporin A.
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P.J.Ellis,
C.K.Carlow,
D.Ma,
P.Kuhn.
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ABSTRACT
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The resistance of the human parasite Brugia malayi to the antiparasitic activity
of cyclosporin A (CsA) may arise from the presence of cyclophilins with
relatively low affinity for the drug. The structure of the complex of B. malayi
cyclophilin (BmCYP-1) and CsA, with eight independent copies in the asymmetric
unit, has been determined at a resolution of 2.7 A. The low affinity of BmCYP-1
for CsA arises from incomplete preorganization of the binding site so that the
formation of a hydrogen bond between His132 of BmCYP-1 and N-methylleucine 9 of
CsA is associated with a shift in the backbone of approximately 1 A in this
region.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.P.Collman,
R.A.Decréau,
Y.Yan,
J.Yoon,
and
E.I.Solomon
(2007).
Intramolecular single-turnover reaction in a cytochrome C oxidase model bearing a Tyr244 mimic.
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J Am Chem Soc,
129,
5794-5795.
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V.Venugopal,
B.Sen,
A.K.Datta,
and
R.Banerjee
(2007).
Structure of cyclophilin from Leishmania donovani at 1.97 A resolution.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
63,
60-64.
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PDB code:
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H.Hu,
C.Q.Huang,
H.L.Liu,
Y.Han,
L.Yu,
and
R.C.Bi
(2005).
Crystallization and preliminary X-ray crystallographic studies of human cyclophilin J.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
61,
216-218.
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D.Ma,
L.S.Nelson,
K.LeCoz,
C.Poole,
and
C.K.Carlow
(2002).
A novel cyclophilin from parasitic and free-living nematodes with a unique substrate- and drug-binding domain.
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J Biol Chem,
277,
14925-14932.
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L.Cavarec,
T.Kamphausen,
B.Dubourg,
I.Callebaut,
F.Lemeunier,
D.Métivier,
J.Feunteun,
G.Fischer,
and
N.Modjtahedi
(2002).
Identification and characterization of Moca-cyp. A Drosophila melanogaster nuclear cyclophilin.
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J Biol Chem,
277,
41171-41182.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
