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Textilinin-1 in complex with trypsin |
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. 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.
Txtln-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.
As part of their work with the Venomics research group, Emma-Karin Millers and Dr Luke Guddat are using X-ray crystallography to determine the 3D structure of protein from Australian venomous snakes to understand how they function. The work is a collaboration between the School of Molecular and Microbial Sciences (UQ), the School of Medicine at Princess Alexandra Hospital, the Queensland Institute of Medical Research (QIMR) and QRX Pharma. Computational calculations necessary to solve macromolecular crystal structures of textilinin-1 (both as a free molecule and in complex with two other proteins) are carried out on the QCIF supercomputer, cyclone.
Contacts
Emma-Karin Millers,
Dr Luke Guddat
School of Molecular and Microbial Sciences,
University of Queensland
Publications
Millers E.K. et. al., 'Crystallization and preliminary X-ray analysis of a Kunitz-type inhibitor, textilinin-1 from Pseudonaja textilis textilis', Acta. Cryst. F62 (2006) 642.
Written by T. Curtis, July 2006.