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| THE INTACT AND CLEAVED HUMAN ANTITHROMBIN-III COMPLEX AS A MODEL FOR SERPIN-PROTEINASE INTERACTIONS |
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| Author(s): SCHREUDER HA, DEBOER B, DIJKEMA R, MULDERS J, THEUNISSEN HJM, GROOTENHUIS PDJ, HOL WGJ |
| Source: NATURE STRUCTURAL BIOLOGY Volume: 1 Issue: 1 Pages: 48-54 Published: JAN 1994 |
| Times Cited: 213 References: 30 |
| Abstract: Antithrombin is a member of the serine proteinase inhibitor (serpin) family which contain a flexible reactive site loop that interacts with, and is cleaved by the target proteinase. In cleaved and latent serpins, the reactive site loop is inserted into a large central beta-sheet in the same molecule, whereas in ovalbumin, a nonfunctional serpin, the reactive site loop is completely exposed and in an alpha-heliacal conformation. however in neither conformation can the reactive site loop bind to target proteinases. here we report the structure of an intact and cleaved human antithrombin complex. The intact reactive site loop is in a novel conformation that seems well suited for interaction with proteinases such as thrombin and blood coagulation factor Xa. |
| Document Type: Article |
| Language: English |
Addresses:
1. UNIV GRONINGEN, BIOSON, RES INST, 9747 AG GRONINGEN, NETHERLANDS
2. ORGANON INT BV, 5340 BH OSS, NETHERLANDS |
| Publisher: NATURE PUBLISHING CO, 345 PARK AVE SOUTH, NEW YORK, NY 10010-1707 |
| Subject Category: Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| IDS Number: NU320 |
| ISSN: 1072-8368 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |