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1a67
From Proteopedia
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a67 OCA], [http://www.ebi.ac.uk/pdbsum/1a67 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a67 RCSB]</span> | ||
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[[Category: thiol proteinase]] | [[Category: thiol proteinase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:34:06 2008'' |
Revision as of 15:34, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CHICKEN EGG WHITE CYSTATIN WILDTYPE, NMR, 16 STRUCTURES
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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