Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Crystal structure of the complex of brugia malayi cyclophilin and cyclosporin a

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Ellis, P. J.
  • Carlow, C. K. S.
  • Ma, D.
  • Kuhn, Peter

publication date

  • January 2000

journal

  • Biochemistry  Journal

abstract

  • 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.

subject areas

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Brugia malayi
  • Crystallography, X-Ray
  • Cyclosporine
  • Humans
  • Hydrogen Bonding
  • Models, Molecular
  • Molecular Sequence Data
  • Open Reading Frames
  • Peptidylprolyl Isomerase
  • Protein Structure, Secondary
  • Recombinant Proteins
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0006-2960

Digital Object Identifier (DOI)

  • 10.1021/bi991730q

PubMed ID

  • 10642184
scroll to property group menus

Additional Document Info

start page

  • 592

end page

  • 598

volume

  • 39

issue

  • 3

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support