ISSN:
0006-3525
Keywords:
conformations
;
x-ray structure
;
protein
;
FK506 binding proteins
;
cyclophilin
;
peptide
;
cyclosporin A
;
FK506, immunosupressants
;
peptidyl-prolyl isomerases
;
immunophilins
;
hydrophilic collapse
;
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
Macrolide ligands that bind FK506 binding proteins and cyclosporins that bind cyclophilins are chemically dissimilar but can share a number of structural and biological properties. Both families of ligands have very different conformations in the free state compared to those adopted when complexed with their binding protein. These transformations involve twisting from cis to trans about specific amide bonds, which result in significant changes in the hydrogen-bonding capabilities of the molecular surfaces. The three-dimensional structure of a new cyclosporin-like ligand (SDZ214-103) is described in the free crystalline state and bound to cyclophilin, and is shown to have a very different conformation from cyclosporin A in the free crystal, but a very similar conformation when bound to cyclophilin. © 1997 John Wiley & Sons, Inc. Biopoly 40: 585-592, 1996
Additional Material:
4 Ill.
Type of Medium:
Electronic Resource
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