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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†,‡


Reference:

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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Official URL:

http://dx.doi.org/10.1021/bi0264521

Abstract

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.

Details

Item Type Articles
CreatorsMohan, C. G., Boix, E., Evans, H. R., Nikolovski, Z., Nogués, M. V., Cuchillo, C. M. and Acharya, R.
DOI10.1021/bi0264521
DepartmentsFaculty of Science > Biology & Biochemistry
RefereedYes
StatusPublished
ID Code18278

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