Crystal structure of the haemopexin-like C-terminal domain of gelatinase A
- 1 November 1995
- journal article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 2 (11), 938-942
- https://doi.org/10.1038/nsb1195-938
Abstract
The crystal structure of the haemopexin-like C-terminal domain of gelatinase A reveals that it is a four-bladed beta-propeller protein. The four blades are arranged around a channel-like opening in which Ca2+ and a Na-Cl+ ion pair are bound.Keywords
This publication has 11 references indexed in Scilit:
- 1.8 å crystal structure of the C-terminal domain of rabbit serum haemopexinStructure, 1995
- Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed β-propellerStructure, 1995
- Mechanism Of Cell Surface Activation Of 72-kDa Type IV CollagenaseJournal of Biological Chemistry, 1995
- A matrix metalloproteinase expressed on the surface of invasive tumour cellsNature, 1994
- Tumor Cell Interactions with the Extracellular Matrix During Invasion and MetastasisAnnual Review of Cell Biology, 1993
- PROCHECK: a program to check the stereochemical quality of protein structuresJournal of Applied Crystallography, 1993
- Matrix Metalloproteinases: A ReviewCritical Reviews in Oral Biology & Medicine, 1993
- The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinasesBiochemical Journal, 1992
- Improved methods for building protein models in electron density maps and the location of errors in these modelsActa Crystallographica Section A Foundations of Crystallography, 1991
- Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2.Proceedings of the National Academy of Sciences, 1989