1f1j

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(New page: 200px<br /> <applet load="1f1j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f1j, resolution 2.35&Aring;" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 14:42, 12 November 2007

Image:1f1j.gif

1f1j, resolution 2.35Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF CASPASE-7 IN COMPLEX WITH ACETYL-ASP-GLU-VAL-ASP-CHO

Overview

BACKGROUND: Peptide inhibitors of caspases have helped define the role of, these cysteine proteases in biology. Structural and biochemical, characterization of the caspase enzymes may contribute to the development, of new drugs for the treatment of caspase-mediated inflammation and, apoptosis. RESULTS: The crystal structure of the previously unpublished, caspase-7 (Csp7; 2.35 A) bound to the reversible tetrapeptide aldehyde, inhibitor acetyl-Asp-Glu-Val-Asp-CHO is compared with crystal structures, of caspases-1 (2.3 A), -3 (2.2 A), and -8 (2.65 A) bound to the same, inhibitor. Csp7 is a close homolog of caspase-3 (Csp3), and these two, caspases possess some quarternary structural characteristics that support, their unique role among the caspase family. However, although Csp3 and, Csp7 are quite similar overall, they were found to have a significantly, different substitution pattern of amino acids in and around the S4-binding, site. CONCLUSIONS: These structures span all three caspase subgroups, and, provide a basis for inferring substrate and inhibitor binding, as well as, selectivity for the entire caspase family. This information will influence, the design of selective caspase inhibitors to further elucidate the role, of caspases in biology and hopefully lead to the design of therapeutic, agents to treat caspase-mediated diseases, such as rheumatoid arthritis, certain neurogenerative diseases and stroke.

About this Structure

1F1J is a Single protein structure of sequence from Homo sapiens with SO4 and ACE as ligands. The following page contains interesting information on the relation of 1F1J with [Caspases]. Full crystallographic information is available from OCA.

Reference

The structures of caspases-1, -3, -7 and -8 reveal the basis for substrate and inhibitor selectivity., Wei Y, Fox T, Chambers SP, Sintchak J, Coll JT, Golec JM, Swenson L, Wilson KP, Charifson PS, Chem Biol. 2000 Jun;7(6):423-32. PMID:10873833

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