Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed β-propeller
Open Access
- 1 June 1995
- Vol. 3 (6), 541-549
- https://doi.org/10.1016/s0969-2126(01)00188-5
Abstract
No abstract availableKeywords
This publication has 45 references indexed in Scilit:
- Fragments of human fibroblast collagenase: interaction with metalloproteinase inhibitors and substratesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1994
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Structural implications for the role of the N terminus in the ‘superactivation’ of collagenasesFEBS Letters, 1994
- Crystallization of the C-terminal Domain of Rabbit Serum HemopexinJournal of Molecular Biology, 1993
- Structural principles for the propeller assembly of β‐sheets: The preference for seven‐fold symmetryProteins-Structure Function and Bioinformatics, 1992
- Production in Escherichia coli of porcine type-I collagenase as a fusion protein with β-galactosidaseGene, 1992
- Crystallization and preliminary X-ray analysis of porcine synovial collagenaseJournal of Molecular Biology, 1989
- A fast algorithm for rendering space-filling molecule picturesJournal of Molecular Graphics, 1988
- A reciprocal-space method for calculating a molecular envelope using the algorithm of B.C. WangActa Crystallographica Section A Foundations of Crystallography, 1987
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983