1uto: Difference between revisions
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Revision as of 17:06, 30 October 2007
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TRYPSIN SPECIFICITY AS ELUCIDATED BY LIE CALCULATIONS, X-RAY STRUCTURES AND ASSOCIATION CONSTANT MEASUREMENTS
OverviewOverview
The variation in inhibitor specificity for five different amine inhibitors, bound to CST, BT, and the cold-adapted AST has been studied by use of, association constant measurements, structural analysis of high-resolution, crystal structures, and the LIE method. Experimental data show that AST, binds the 1BZA and 2BEA inhibitors 0.8 and 0.5 kcal/mole more strongly, than BT. However, structural interactions and orientations of the, inhibitors within the S1 site have been found to be virtually identical in, the three enzymes studied. For example, the four water molecules in the, inhibitor-free structures of AST and BT are channeled into similar, positions in the S1 site, and the nitrogen atom(s) of the inhibitors are, found in two cationic binding sites denoted Position1 and Position2. The, ... [(full description)]
About this StructureAbout this Structure
1UTO is a [Single protein] structure of sequence from [Bos taurus] with CA, PEA and GOL as [ligands]. Active as [Trypsin], with EC number [3.4.21.4]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Trypsin specificity as elucidated by LIE calculations, X-ray structures, and association constant measurements., Leiros HK, Brandsdal BO, Andersen OA, Os V, Leiros I, Helland R, Otlewski J, Willassen NP, Smalas AO, Protein Sci. 2004 Apr;13(4):1056-70. PMID:15044735
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