The Crystal Structure of Eosinophil Cationic Protein in Complex with 2‘,5‘-ADP at 2.0 Å Resolution Reveals the Details of the Ribonucleolytic Active Site†,‡
Mohan, C. G., Boix, E., Evans, H. R., Nikolovski, Z., Nogués, M. V., Cuchillo, C. M. and Acharya, R., 2002. The Crystal Structure of Eosinophil Cationic Protein in Complex with 2‘,5‘-ADP at 2.0 Å Resolution Reveals the Details of the Ribonucleolytic Active Site†,‡. Biochemistry, 41 (40), pp. 12100-12106.
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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 Å) 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 hydrogen bond interactions with the phosphate at the P1 site, while His-128 interacts with the purine ring at the B2 site. A new phosphate binding site, P-1, has been identified which involves Arg-34. This study is the first detailed structural analysis of the nucleotide recognition site in ECP and provides a starting point for the understanding of its substrate specificity and low catalytic efficiency compared with that of the eosinophil-derived neurotoxin (EDN), a close homologue.
|Creators||Mohan, C. G., Boix, E., Evans, H. R., Nikolovski, Z., Nogués, M. V., Cuchillo, C. M. and Acharya, R.|
|Departments||Faculty of Science > Biology & Biochemistry|
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