1c79: Difference between revisions
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<StructureSection load='1c79' size='340' side='right'caption='[[1c79]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1c79' size='340' side='right'caption='[[1c79]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1c79]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1c79]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C79 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1c76|1c76]], [[1c77|1c77]], [[1c78|1c78]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1c76|1c76]], [[1c77|1c77]], [[1c78|1c78]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aureolysin Aureolysin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.29 3.4.24.29] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c79 OCA], [https://pdbe.org/1c79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c79 RCSB], [https://www.ebi.ac.uk/pdbsum/1c79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c79 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/SAK_STAAU SAK_STAAU]] Potent plasminogen activator that converts plasminogen into plasmin. It forms a 1:1 complex with plasmin, which in turn activates other plasminogen molecules. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 13:33, 14 July 2021
STAPHYLOKINASE (SAK) DIMERSTAPHYLOKINASE (SAK) DIMER
Structural highlights
Function[SAK_STAAU] Potent plasminogen activator that converts plasminogen into plasmin. It forms a 1:1 complex with plasmin, which in turn activates other plasminogen molecules. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedStaphylokinase (SAK) is a 15.5-kDa protein from Staphylococcus aureus that activates plasminogen by forming a 1 : 1 complex with plasmin. Recombinant SAK has been shown in clinical trials to induce fibrin-specific clot lysis in patients with acute myocardial infarction. However, SAK elicits high titers of neutralizing antibodies. Biochemical and protein engineering studies have demonstrated the feasibility of generating SAK variants with reduced antigenicity yet intact thrombolytic potency. Here, we present X-ray crystallographic evidence that the SAK(S41G) mutant may assume a dimeric structure. This dimer model, at 2.3-A resolution, could explain a major antigenic epitope (residues A72-F76 and residues K135-K136) located in the vicinity of the dimer interface as identified by phage-display. These results suggest that SAK antigenicity may be reduced by eliminating dimer formation. We propose several potential mutation sites at the dimer interface that may further reduce the antigenicity of SAK. Crystal structure of a staphylokinase: variant a model for reduced antigenicity.,Chen Y, Song G, Jiang F, Feng L, Zhang X, Ding Y, Bartlam M, Yang A, Ma X, Ye S, Liu Y, Tang H, Song H, Rao Z Eur J Biochem. 2002 Jan;269(2):705-11. PMID:11856331[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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