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| CRYSTAL-STRUCTURE OF AN UNCLEAVED SERPIN REVEALS THE CONFORMATION OF AN INHIBITORY REACTIVE LOOP |
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| Author(s): WEI AZ, RUBIN H, COOPERMAN BS, CHRISTIANSON DW |
| Source: NATURE STRUCTURAL BIOLOGY Volume: 1 Issue: 4 Pages: 251-258 Published: APR 1994 |
| Times Cited: 151 References: 55 |
| Abstract: The three-dimensional structure of an uncleaved serpin, a variant of human antichymotrypsin engineered to be an inhibitor of human neutrophil elastase, has been determined by X-ray crystallographic methods and is currently being refined at 2.5 Angstrom resolution. It contains an intact reactive loop in a distorted helical conformation. A comparison of the current model with that of its cleaved counterpart suggests that the conformational 'stress' of the serpin in its uncleaved and uncomplexed state may not be confined solely to the reactive loop or beta-sheet A. It is intriguing that strand s4A is not pre-inserted into beta-sheet A of the native serpin, and this has profound implications for the mechanism of serpin function. |
| Document Type: Article |
| Language: English |
Addresses:
1. UNIV PENN, DEPT CHEM, PHILADELPHIA, PA 19104 USA
2. UNIV PENN, DEPT MED, PHILADELPHIA, PA 19104 USA |
| Publisher: NATURE PUBLISHING CO, 345 PARK AVE SOUTH, NEW YORK, NY 10010-1707 |
| Subject Category: Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| IDS Number: NU323 |
| ISSN: 1072-8368 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |