1utl

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Revision as of 15:31, 29 October 2007

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spinqualitylabelsall models 1utl, resolution 1.7Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

TRYPSIN SPECIFICITY AS ELUCIDATED BY LIE CALCULATIONS, X-RAY STRUCTURES AND ASSOCIATION CONSTANT MEASUREMENTS

Overview

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 Structure

1UTL is a [Single protein] structure of sequence from [[1]] with CA, PRA and MPD as [ligands]. Active as [[2]], with EC number [3.4.21.4]. Full crystallographic information is available from [OCA].

Reference

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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