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1c4p
From Proteopedia
Revision as of 17:06, 20 August 2014 by OCA (Talk | contribs)
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Streptokinase, a 47 kDa secreted protein of hemolytic strains of streptococci, is a human plasminogen activator and contains three structural domains linked by flexible loops. We describe here the crystal structure of the isolated streptokinase middle (SKbeta) domain determined at 2.4 A resolution. Among the functionally important structural features is a putative binding site for a kringle domain of plasminogen located at the tip of a fully exposed hairpin loop. The distribution of genetically conserved residues of SKbeta is strongly correlated with their functions. The extensive interface of the SKbeta dimer suggests that such dimers may also exist in solution for free SKbeta.
Crystal structure of streptokinase beta-domain.,Wang X, Tang J, Hunter B, Zhang XC FEBS Lett. 1999 Oct 1;459(1):85-9. PMID:10508922[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Wang X, Tang J, Hunter B, Zhang XC. Crystal structure of streptokinase beta-domain. FEBS Lett. 1999 Oct 1;459(1):85-9. PMID:10508922
