2001 Fiscal Year Final Research Report Summary

Substrate binding mechanism of heparan sulfate N-sulfotransferase

Research Project

Project/Area Number	12680611
Research Category	Grant-in-Aid for Scientific Research (C)
Allocation Type	Single-year Grants
Section	一般
Research Field	Structural biochemistry
Research Institution	KYUSHU UNIVERSITY (2001) Osaka University (2000)
Principal Investigator	KAKUTA Yoshimitsu Kyushu University, 大学院・農学研究院, 助教授 (00314360)
Project Period (FY)	2000 – 2001
Keywords	heparan sulfate / sulfotransferase / X線結晶構造解析
Research Abstract	Heparan sulfates are the complex chains of sulfated glycosaminoglycans. Heparan sulfate chains are ubiquitously present as proteoglycans on cell surfaces and in extracellular matrix. They have been increasingly implicated in various biological processes including cell growth, cell differentiation, blood coagulation, and viral and bacterial infections. Heparan sulfate sulfotransferase (NST) catalyzes transfer of the 5'- sulfuryl group of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the amino group of heparan sulfate. We determined 2A^^゜ resolution structure of NST-PAPS complex. The structure indicate that residues Lys614, Lys833, Lys676 and GLU642 play an important role for PAPS binding and enzyme activity.

(6 results)