High-Resolution Crystal Structure of the Snake Venom Metalloproteinase BaP1 Complexed with a Peptidomimetic: Insight into Inhibitor Binding-Reference-Cited by-同舟云学术

High-Resolution Crystal Structure of the Snake Venom Metalloproteinase BaP1 Complexed with a Peptidomimetic: Insight into Inhibitor Binding

Published:2009-06-15 Issue:26 Volume:48 Page:6166-6174
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Lingott Torsten¹,Schleberger Christian¹,Gutiérrez José María²,Merfort Irmgard¹

Affiliation:

1. Department of Pharmaceutical Biology and Biotechnology, Institute of Pharmaceutical Sciences, Albert-Ludwigs-Universität, Stefan-Meier-Strasse 19, 79104 Freiburg im Breisgau, Germany

2. Clodomiro Picado Institute, Faculty of Microbiology, University of Costa Rica, San José, Costa Rica

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi9002315

Reference53 articles.

1. [21] Snake venom metalloendopeptidases: Reprolysins

2. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the ‘metzincins’

3. Structural Aspects of the Metzincin Clan of Metalloendopeptidases

4. The metzincins - Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc-peptidases

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