Mapping of the plasminogen binding site of streptokinase with short synthetic peptides

Protein Science : a Publication of the Protein Society
D NihalaniGirish Sahni

Abstract

Although several recent studies employing various truncated fragments of streptokinase (SK) have demonstrated that the high-affinity interactions of this protein with human plasminogen (HPG) to form activator complex (SK-HPG) are located in the central region of SK, the exact location and nature of such HPG interacting site(s) is still unclear. In order to locate the "core" HPG binding ability in SK, we focused on the primary structure of a tryptic fragment of SK derived from the central region (SK143-293) that could bind as well as activate HPG, albeit at reduced levels in comparison to the activity of the native, full-length protein. Because this fragment was refractory to further controlled proteolysis, we took recourse to a synthetic peptide approach wherein the HPG interacting properties of 16 overlapping 20-mer peptides derived from this region of SK were examined systematically. Only four peptides from this set, viz., SK234-253, SK254-273, SK274-293, and SK263-282, together representing the contiguous sequence SK234-293, displayed HPG binding ability. This was established by a specific HPG-binding ELISA as well as by dot blot assay using 125I-labeled HPG. These results showed that the minimal sequence with HPG binding fu...Continue Reading

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Citations

Oct 29, 1998·Protein Science : a Publication of the Protein Society·F Conejero-LaraC P Ponting
Feb 27, 1999·Protein Science : a Publication of the Protein Society·A I AzuagaC M Dobson
Jul 25, 2003·Proceedings of the National Academy of Sciences of the United States of America·Inna P GladyshevaGuy L Reed
Oct 6, 1999·FEBS Letters·X WangX C Zhang
Jun 25, 2004·The Journal of Biological Chemistry·Paul D BoxrudPaul E Bock

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