1a67 | pdb_00001a67
CHICKEN EGG WHITE CYSTATIN WILDTYPE, NMR, 16 STRUCTURES
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Overview
The solution structures of the phosphorylated form of native chicken, cystatin and the recombinant variant AEF-S1M-M29I-M89L were determined by, 2D, 3D and 4D-NMR. The structures turn out to be very similar, despite the, substitutions and the phosphorylation of the wild-type. Their dominant, feature is a five-stranded beta-sheet, which is wrapped around a five-turn, alpha-helix, as shown by X-ray crystallographic studies of wild-type, chicken cystatin. However, the NMR analysis shows that the second helix, observed in the crystal is not present in solution. The phosphorylation, occurs at S80, which is located in a flexible region. For this reason, very few effects on the structure are observed. Comparison of structures, of the unphosphorylated variant and the wild-type shows small effects on, H84 which is located in the supposed recognition site of the serine, kinase. This recognition site appears to be well structured as a large, loop-containing bulge of the beta-sheet. The N termini of both mutants, which contribute to a large extent to the binding to the proteinase, are, very flexible. A loop structure involving the residues L7 to A10 as found, in related inhibitors, such as in the kininogen domains 2 and 3, is not, sufficiently populated to be observed.
About this Structure
1A67 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
The structures of native phosphorylated chicken cystatin and of a recombinant unphosphorylated variant in solution., Dieckmann T, Mitschang L, Hofmann M, Kos J, Turk V, Auerswald EA, Jaenicke R, Oschkinat H, J Mol Biol. 1993 Dec 20;234(4):1048-59. PMID:8263912
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