A Peptide Model for the Heparin Binding Site on Antithrombin III,

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Abstract:

The 432 amino acid glycoprotein Antithrombin III ATIII regulates several key steps in the blood clotting cascade by inhibiting serine proteases such as thrombin and factor X sub a. The rate by which ATIII inhibits these enzymes is accelerated 1000-fold by binding to a specific polysaccharide sequence within the carbohydrate chains of heparin. Heparin is a heterogeneous polysulfated proteoglycan, the saccharide portion of which is commonly prescribed in the treatment of thrombosis.

Author(s):
Coffman, Annemarie I. ; Lansbury, Peter T., Jr
Author Organization(s):
MASSACHUSETTS INST OF TECH CAMBRIDGE
Supplementary Note:
This article is from 'Peptides. Chemistry and Biology: Proceedings of the American Peptide Symposium (12th) Held in Cambridge, Massachusetts on 16-21 June 1991', AD-A256 113, p420-422.
Pagination:
0003

Security Markings

DOCUMENT & CONTEXTUAL SUMMARY

Distribution:
Approved For Public Release

RECORD

Collection: TR
Identifying Numbers
Monitor Series:
USAMRDC
 Subject Terms
Communities of Interest:
No COI(s) Identified
Descriptor(s):
*THROMBIN, *HEPARIN, *ANTICOAGULANTS, ENZYME INHIBITORS, AMINO ACIDS, THROMBOSIS, PEPTIDES, BLOOD PLASMA, SERINE
Field(s)/Group(s):
Biochemistry, Pharmacology
Keyword(s):
Antithrombin 3, Component Reports
Report Date:
1992 Jan 01