Crystallisation and preliminary X-ray diffraction studies of cyclophilin-tetrapeptide and cyclophilin-cyclosporin complexes

M Zurini; J Kallen; V Mikol; G Pfluegl; J N Jansonius; M D Walkinshaw

doi:10.1016/0014-5793(90)80507-f

Crystallisation and preliminary X-ray diffraction studies of cyclophilin-tetrapeptide and cyclophilin-cyclosporin complexes

FEBS Lett. 1990 Dec 10;276(1-2):63-6. doi: 10.1016/0014-5793(90)80507-f.

Authors

M Zurini¹, J Kallen, V Mikol, G Pfluegl, J N Jansonius, M D Walkinshaw

Affiliation

¹ Preclinical Research, Sandoz Pharma AG, Basel, Switzerland.

PMID: 2265714
DOI: 10.1016/0014-5793(90)80507-f

Abstract

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.

MeSH terms

Amino Acid Isomerases / chemistry
Amino Acid Isomerases / isolation & purification
Amino Acid Isomerases / metabolism*
Amino Acid Sequence
Carrier Proteins / chemistry
Carrier Proteins / isolation & purification
Carrier Proteins / metabolism*
Coumarins / metabolism*
Crystallization
Cyclosporins / metabolism*
Molecular Sequence Data
Oligopeptides / metabolism*
Peptidylprolyl Isomerase
Protein Binding
Protein Conformation
X-Ray Diffraction

Substances

Carrier Proteins
Coumarins
Cyclosporins
Oligopeptides
N-acetyl-alanyl-alanyl-prolyl-alanyl-amidomethylcoumarin
Amino Acid Isomerases
Peptidylprolyl Isomerase