Crystallisation and preliminary X-ray diffraction studies of cyclophilin-tetrapeptide and cyclophilin-cyclosporin complexes.
Recombinant human cyclophilin has been co-crystallised with a number of peptides to give crystals suitable for X-ray analysis. The crystal complexes for which heavy-atom derivatives have been prepared and X-ray data collected are: cyclophilin with N-acetyl-Ala-Ala-Pro-Ala-amidomethyl-coumarin (I) which crystallises in space group P2(1)2(1)2(1) with a = 108.2, b = 123.0, c = 35.8 A, and cyclophilin with cyclosporin (II) which crystallises as tetragonal plates in space group P4(1)2(1)2 or P4(3)2(1)2 with a = b = 94.98, c = 278.55 A.
Zurini
M
M
Preclinical Research, Sandoz Pharma AG, Basel, Switzerland.
Kallen
J
J
Mikol
V
V
Pfluegl
G
G
Jansonius
J N
JN
Walkinshaw
M D
MD
D000591:Amino Acid Isomerases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D003374:Coumarins / Q000378:metabolism*; D003460:Crystallization; D003524:Cyclosporins / Q000378:metabolism*; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism*; D019696:Peptidylprolyl Isomerase; D011485:Protein Binding; D011487:Protein Conformation; D014961:X-Ray Diffraction
D002352:Carrier Proteins; D003374:Coumarins; D003524:Cyclosporins; D009842:Oligopeptides; C066763:N-acetyl-alanyl-alanyl-prolyl-alanyl-amidomethylcoumarin; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase