1h1h: Difference between revisions
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Revision as of 16:20, 30 October 2007
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CRYSTAL STRUCTURE OF EOSINOPHIL CATIONIC PROTEIN IN COMPLEX WITH 2',5'-ADP AT 2.0 A RESOLUTION REVEALS THE DETAILS OF THE RIBONUCLEOLYTIC ACTIVE SITE
OverviewOverview
Eosinophil cationic protein (ECP) is a component of the eosinophil granule, matrix. It shows marked toxicity against helminth parasites, bacteria, single-stranded RNA viruses, and host epithelial cells. Secretion of human, ECP is related to eosinophil-associated allergic, asthmatic, and, inflammatory diseases. ECP belongs to the pancreatic ribonuclease, superfamily of proteins, and the crystal structure of ECP in the, unliganded form (determined previously) exhibited a conserved RNase A fold, [Boix, E., et al. (1999) Biochemistry 38, 16794-16801]. We have now, determined a high-resolution (2.0 A) crystal structure of ECP in complex, with adenosine 2',5'-diphosphate (2',5'-ADP) which has revealed the, details of the ribonucleolytic active site. Residues Gln-14, His-15, and, Lys-38 make ... [(full description)]
About this StructureAbout this Structure
1H1H is a [Single protein] structure of sequence from [Homo sapiens] with A2P as [ligand]. Structure known Active Site: A2P. Full crystallographic information is available from [OCA].
ReferenceReference
The crystal structure of eosinophil cationic protein in complex with 2',5'-ADP at 2.0 A resolution reveals the details of the ribonucleolytic active site., Mohan CG, Boix E, Evans HR, Nikolovski Z, Nogues MV, Cuchillo CM, Acharya KR, Biochemistry. 2002 Oct 8;41(40):12100-6. PMID:12356310
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