1c78: Difference between revisions
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|SITE= | |SITE= | ||
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|ACTIVITY= [http://en.wikipedia.org/wiki/Aureolysin Aureolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.29 3.4.24.29] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aureolysin Aureolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.29 3.4.24.29] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1c76|1C76]], [[1c77|1C77]], [[1c79|1C79]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c78 OCA], [http://www.ebi.ac.uk/pdbsum/1c78 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c78 RCSB]</span> | |||
}} | }} | ||
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[[Category: beta-grasp family]] | [[Category: beta-grasp family]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:15:59 2008'' | ||
Revision as of 19:16, 30 March 2008
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| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Aureolysin, with EC number 3.4.24.29 | ||||||
| Related: | 1C76, 1C77, 1C79
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STAPHYLOKINASE (SAK) DIMER
OverviewOverview
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.
About this StructureAbout this Structure
1C78 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
ReferenceReference
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
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