1a67

<StructureSection load='1a67' size='340' side='right'caption='[[1a67]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1a67]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A67 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A67 FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1a67 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a67 RCSB], [http://www.ebi.ac.uk/pdbsum/1a67 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1a67 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CYT_CHICK CYT_CHICK]] This protein binds tightly to and inhibits a variety of thiol proteases including ficin, papain, and cathepsins B, C, H, and L. Although isolated from egg white, it is also present in serum.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:8263912</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1a67" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Auerswald, E A]]

[[Category: Dieckmann, T]]

[[Category: Hofmann, M]]

[[Category: Jaenicke, R]]

[[Category: Kos, J]]

[[Category: Mitschang, L]]

[[Category: Oschkinat, H]]

[[Category: Turk, V]]

[[Category: Thiol proteinase]]