Document Detail


X-ray structure of a cyclophilin B/cyclosporin complex: comparison with cyclophilin A and delineation of its calcineurin-binding domain.
MedLine Citation:
PMID:  8197205     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The crystal structure of a complex between recombinant human cyclophilin B (CypB) and a cyclosporin A (CsA) analog has been determined and refined at 1.85-A resolution to a crystallographic R factor of 16.0%. The overall structures of CypB and of cyclophilin A (CypA) are similar; however, significant differences occur in two loops and at the N and C termini. The CsA-binding pocket in CypB has the same structure as in CypA and cyclosporin shows a similar bound conformation and network of interactions in both CypB and CypA complexes. The network of the water-mediated contacts is also essentially conserved. The higher potency of the CypB/CsA complex versus CypA/CsA in inhibiting the Ca(2+)- and calmodulin-dependent protein phosphatase calcineurin is discussed in terms of the structural differences between the two complexes. The three residues Arg90, Lys113, and Ala128 and the loop containing Arg158 on the surface of CypB are likely to modulate the differences in calcineurin inhibition between CypA and CypB.
Authors:
V Mikol; J Kallen; M D Walkinshaw
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Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  91     ISSN:  0027-8424     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  1994 May 
Date Detail:
Created Date:  1994-06-27     Completed Date:  1994-06-27     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  5183-6     Citation Subset:  IM    
Affiliation:
Preclinical Research, Sandoz AG, Basel, Switzerland.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Isomerases / chemistry*,  metabolism
Amino Acid Sequence
Binding Sites
Calcineurin
Calmodulin-Binding Proteins / antagonists & inhibitors,  metabolism*
Carrier Proteins / chemistry*,  metabolism
Crystallography, X-Ray
Cyclophilins*
Cyclosporine / chemistry*,  metabolism
Humans
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Peptidylprolyl Isomerase
Phosphoprotein Phosphatases / antagonists & inhibitors,  metabolism*
Protein Conformation
Sequence Homology, Amino Acid
Chemical
Reg. No./Substance:
0/Calmodulin-Binding Proteins; 0/Carrier Proteins; 137497-17-7/cyclophilin B; 59865-13-3/Cyclosporine; EC 3.1.3.16/Calcineurin; EC 3.1.3.16/Phosphoprotein Phosphatases; EC 5.1.1.-/Amino Acid Isomerases; EC 5.2.1.-/Cyclophilins; EC 5.2.1.8/Peptidylprolyl Isomerase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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