1a67: Difference between revisions
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'''CHICKEN EGG WHITE CYSTATIN WILDTYPE, NMR, 16 STRUCTURES''' | {{Structure | ||
|PDB= 1a67 |SIZE=350|CAPTION= <scene name='initialview01'>1a67</scene> | |||
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|LIGAND= | |||
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'''CHICKEN EGG WHITE CYSTATIN WILDTYPE, NMR, 16 STRUCTURES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1A67 is a [ | 1A67 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A67 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8263912 8263912] | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Oschkinat, H.]] | [[Category: Oschkinat, H.]] | ||
[[Category: Turk, V.]] | [[Category: Turk, V.]] | ||
[[Category: | [[Category: kininogen]] | ||
[[Category: proteinase inhibitor]] | [[Category: proteinase inhibitor]] | ||
[[Category: | [[Category: steffin]] | ||
[[Category: thiol proteinase]] | [[Category: thiol proteinase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:53:29 2008'' | ||
Revision as of 07:53, 20 March 2008
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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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