Crystallization and crystallographic studies of kallistatin
- Shanghai Jiaotong University School of Medicine (Room 1006, Building 2, No 280, South Chongqing Road), Shanghai 200025, People’s Republic of (China)
The crystallization of human kallistatin in the relaxed conformation is reported. Kallistatin is a serine protease inhibitor (serpin) which specifically inhibits human tissue kallikrein; however, its inhibitory activity is inhibited by heparin. In order to elucidate the underlying mechanism, recombinant human kallistatin was prepared in Escherichia coli and the protein was crystallized by the sitting-drop vapour-diffusion method. X-ray diffraction data were collected to 1.9 Å resolution. The crystals were found to belong to space group P6{sub 1}, with unit-cell parameters a = 113.51, b = 113.51, c = 76.17 Å. Initial analysis indicated that the crystallized kallistatin was in a relaxed conformation, with its reactive-centre loop inserted in the central β-sheet.
- OSTI ID:
- 22420139
- Journal Information:
- Acta Crystallographica. Section F, Structural Biology Communications, Vol. 71, Issue Pt 9; Other Information: PMCID: PMC4555919; PMID: 26323298; PUBLISHER-ID: hc5193; PUBLISHER-ID: S2053230X15012893; OAI: oai:pubmedcentral.nih.gov:4555919; Copyright (c) Lin et al. 2015; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA); ISSN 2053-230X
- Country of Publication:
- United States
- Language:
- English
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