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Crystallization and preliminary X-ray analysis of a Kunitz-type inhibitor, textilinin-1 fromPseudonaja textilis textilis
- Source :
- Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62:642-645
- Publication Year :
- 2006
- Publisher :
- International Union of Crystallography (IUCr), 2006.
-
Abstract
- Textilinin-1 (Txln-1), a Kunitz-type serine protease inhibitor, is a 59-amino-acid polypeptide isolated from the venom of the Australian Common Brown snake Pseudonaja textilis textilis. This molecule has been suggested as an alternative to aprotinin, also a Kunitz-type serine protease inhibitor, for use as an anti-bleeding agent in surgical procedures. Txln-1 shares only 47% amino-acid identity to aprotinin; however, six cysteine residues in the two peptides are in conserved locations. It is therefore expected that the overall fold of these molecules is similar but that they have contrasting surface features. Here, the crystallization of recombinant textilinin-1 (rTxln-1) as the free molecule and in complex with bovine trypsin (229 amino acids) is reported. Two organic solvents, phenol and 1,4-butanediol, were used as additives to facilitate the crystallization of free rTxln-1. Crystals of the rTxln-1-bovine trypsin complex diffracted to 2.0 angstroms resolution, while crystals of free rTxln-1 diffracted to 1.63 angstroms resolution.
- Subjects :
- Biophysics
Crystallography, X-Ray
complex mixtures
Biochemistry
law.invention
Pseudonaja textilis
Aprotinin
X-Ray Diffraction
Structural Biology
law
Genetics
medicine
Animals
Trypsin
Amino Acid Sequence
Elapidae
Fibrinolysin
Crystallization
Elapid Venoms
chemistry.chemical_classification
Serine protease
Sequence Homology, Amino Acid
biology
Chemistry
Condensed Matter Physics
biology.organism_classification
Amino acid
enzymes and coenzymes (carbohydrates)
Brown snake
Crystallization Communications
biological sciences
health occupations
biology.protein
bacteria
Cattle
Cysteine
medicine.drug
Subjects
Details
- ISSN :
- 17443091
- Volume :
- 62
- Database :
- OpenAIRE
- Journal :
- Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Accession number :
- edsair.doi.dedup.....5010af1a61839c0abc56ae451b2a594e