1iau

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Revision as of 15:21, 12 November 2007

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spinqualitylabelsall models 1iau, resolution 2.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

HUMAN GRANZYME B IN COMPLEX WITH AC-IEPD-CHO

Overview

BACKGROUND: Granzyme B, one of the most abundant granzymes in cytotoxic, T-lymphocyte (CTL) granules, and members of the caspase (cysteine aspartyl, proteinases) family have a unique cleavage specificity for aspartic acid, in P1 and play critical roles in the biochemical events that culminate in, cell death. RESULTS: We have determined the three-dimensional structure of, the complex of the human granzyme B with a potent tetrapeptide aldehyde, inhibitor. The Asp-specific S1 subsite of human granzyme B is, significantly larger and less charged than the corresponding Asp-specific, site in the apoptosis-promoting caspases, and also larger than the, corresponding subsite in rat granzyme B. CONCLUSIONS: The above, differences account for the variation in substrate specificity among, granzyme B, other serine proteases and the caspases, and enable the design, of specific inhibitors that can probe the physiological functions of these, proteins and the disease states with which they are associated.

About this Structure

1IAU is a Single protein structure of sequence from Homo sapiens with NAG, ZN and ACE as ligands. Active as Granzyme B, with EC number 3.4.21.79 Full crystallographic information is available from OCA.

Reference

The three-dimensional structure of human granzyme B compared to caspase-3, key mediators of cell death with cleavage specificity for aspartic acid in P1., Rotonda J, Garcia-Calvo M, Bull HG, Geissler WM, McKeever BM, Willoughby CA, Thornberry NA, Becker JW, Chem Biol. 2001 Apr;8(4):357-68. PMID:11325591

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