1a67

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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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'''CHICKEN EGG WHITE CYSTATIN WILDTYPE, NMR, 16 STRUCTURES'''
'''CHICKEN EGG WHITE CYSTATIN WILDTYPE, NMR, 16 STRUCTURES'''
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[[Category: Oschkinat, H.]]
[[Category: Oschkinat, H.]]
[[Category: Turk, V.]]
[[Category: Turk, V.]]
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[[Category: kininogen]]
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[[Category: Kininogen]]
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[[Category: proteinase inhibitor]]
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[[Category: Proteinase inhibitor]]
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[[Category: steffin]]
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[[Category: Steffin]]
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[[Category: thiol proteinase]]
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[[Category: Thiol proteinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:52:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:34:06 2008''
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Revision as of 06:52, 2 May 2008

Template:STRUCTURE 1a67

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 Page seeded by OCA on Fri May 2 09:52:23 2008

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