Crystal structure of a 16 kda double-headed bowman-birk trypsin inhibitor from barley seeds at 1.9 Å resolution
- 12 November 1999
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 293 (5) , 1133-1144
- https://doi.org/10.1006/jmbi.1999.3239
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- The role of the P2′ position of Bowman-Birk proteinase inhibitor in the inhibition of trypsin: Studies on P2′ variation in cyclic peptides encompassing the reactive site loopBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1999
- The role of threonine in the P 2 position of bowman-birk proteinase inhibitors: studies on P 2 variation in cyclic peptides encompassing the reactive site loop 1 1Edited by A. R. FershtJournal of Molecular Biology, 1998
- Rapid refinement of protein interfaces incorporating solvation: application to the docking problemJournal of Molecular Biology, 1998
- Kunitz-type soybean trypsin inhibitor revisited: refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activatorJournal of Molecular Biology, 1998
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Crystallographic Refinement of Bowman-Birk Type Protease Inhibitor A-II from Peanut (Arachis hypogaea) at 2·3 Å ResolutionJournal of Molecular Biology, 1993
- Crystal structure of a Kunitz-type trypsin inhibitor from Erythrina coffra seedsJournal of Molecular Biology, 1991
- CHAIN — A crystallographic modeling programJournal of Molecular Graphics, 1988
- Trypsin inhibitory activity of a polypeptide isolated from red kidney beans, that also enhances lymphocyte stimulationBiochemical and Biophysical Research Communications, 1979