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1c79

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Revision as of 00:52, 25 December 2014

STAPHYLOKINASE (SAK) DIMER

Structural highlights

1c79 is a 2 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1c76, 1c77, 1c78
Activity:	Aureolysin, with EC number 3.4.24.29
Resources:	FirstGlance, OCA, RCSB, PDBsum

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 PubMed

Staphylokinase (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

↑ 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. Crystal structure of a staphylokinase: variant a model for reduced antigenicity. Eur J Biochem. 2002 Jan;269(2):705-11. PMID:11856331

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1c79"

@@ Line 7: / Line 7: @@
 <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=1c79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c79 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c79 RCSB], [http://www.ebi.ac.uk/pdbsum/1c79 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

1c79

From Proteopedia

Revision as of 00:52, 25 December 2014

STAPHYLOKINASE (SAK) DIMER

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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