2c02

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[[Category: sensory transduction]]
[[Category: sensory transduction]]
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Revision as of 14:48, 30 October 2007


2c02, resolution 2.00Å

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CRYSTAL STRUCTURES OF EOSINOPHIL-DERIVED NEUROTOXIN IN COMPLEX WITH THE INHIBITORS 5'-ATP, AP3A, AP4A AND AP5A

Overview

Eosinophil-derived neurotoxin (EDN) is a catalytically proficient member, of the pancreatic ribonuclease superfamily secreted along with other, eosinophil granule proteins during innate host defense responses and, various eosinophil-related inflammatory and allergic diseases. The, ribonucleolytic activity of EDN is central to its antiviral and neurotoxic, activities and possibly to other facets of its biological activity. To, probe the importance of this enzymatic activity further, specific, inhibitors will be of great aid. Derivatives of 5'-ADP are among the most, potent inhibitors currently known. Here, we use X-ray crystallography to, investigate the binding of four natural nucleotides containing this, moiety. 5'-ATP binds in two alternative orientations, one occupying the B2, subsite ... [(full description)]

About this Structure

2C02 is a [Single protein] structure of sequence from [Homo sapiens] with ADP and ACY as [ligands]. Active as [Pancreatic ribonuclease], with EC number [3.1.27.5]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Crystal structures of eosinophil-derived neurotoxin (EDN) in complex with the inhibitors 5'-ATP, Ap3A, Ap4A, and Ap5A., Baker MD, Holloway DE, Swaminathan GJ, Acharya KR, Biochemistry. 2006 Jan 17;45(2):416-26. PMID:16401072

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