1a67: Difference between revisions

← Older edit Newer edit →

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 ==CHICKEN EGG WHITE CYSTATIN WILDTYPE, NMR, 16 STRUCTURES==
-<StructureSection load='1a67' size='340' side='right'caption='[[1a67]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''>
+<StructureSection load='1a67' size='340' side='right'caption='[[1a67]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1a67]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/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'>[https://proteopedia.org/fgij/fg.htm?mol=1a67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a67 OCA], [https://pdbe.org/1a67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a67 RCSB], [https://www.ebi.ac.uk/pdbsum/1a67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a67 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a67 OCA], [https://pdbe.org/1a67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a67 RCSB], [https://www.ebi.ac.uk/pdbsum/1a67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a67 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://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.
+[https://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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 18: / Line 19: @@
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a67 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== 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>
-</div>
-<div class="pdbe-citations 1a67" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Gallus gallus]]
 [[Category: Large Structures]]
-[[Category: Auerswald, E A]]
+[[Category: Auerswald EA]]
-[[Category: Dieckmann, T]]
+[[Category: Dieckmann T]]
-[[Category: Hofmann, M]]
+[[Category: Hofmann M]]
-[[Category: Jaenicke, R]]
+[[Category: Jaenicke R]]
-[[Category: Kos, J]]
+[[Category: Kos J]]
-[[Category: Mitschang, L]]
+[[Category: Mitschang L]]
-[[Category: Oschkinat, H]]
+[[Category: Oschkinat H]]
-[[Category: Turk, V]]
+[[Category: Turk V]]
-[[Category: Kininogen]]
-[[Category: Proteinase inhibitor]]
-[[Category: Steffin]]
-[[Category: Thiol proteinase]]