1qmt
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(New page: 200px<br /> <applet load="1qmt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qmt, resolution 2.40Å" /> '''RECOMBINANT HUMAN E...)
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Revision as of 16:48, 12 November 2007
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RECOMBINANT HUMAN EOSINOPHIL CATIONIC PROTEIN
Overview
Eosinophil cationic protein (ECP) is located in the matrix of the, eosinophil's large specific granule and has marked toxicity for a variety, of helminth parasites, hemoflagellates, bacteria, single-stranded RNA, virus, and mammalian cells and tissues. It belongs to the bovine, pancreatic ribonuclease A (RNase A) family and exhibits ribonucleolytic, activity which is about 100-fold lower than that of a related eosinophil, ribonuclease, the eosinophil-derived neurotoxin (EDN). The crystal, structure of human ECP, determined at 2.4 A, is similar to that of RNase A, and EDN. It reveals that residues Gln-14, His-15, Lys-38, Thr-42, and, His-128 at the active site are conserved as in all other RNase A, homologues. Nevertheless, evidence for considerable divergence of ECP is, also implicit in the structure. Amino acid residues Arg-7, Trp-10, Asn-39, His-64, and His-82 appear to play a key part in the substrate specificity, and low catalytic activity of ECP. The structure also shows how the, cationic residues are distributed on the surface of the ECP molecule that, may have implications for an understanding of the cytotoxicity of this, enzyme.
About this Structure
1QMT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of eosinophil cationic protein at 2.4 A resolution., Boix E, Leonidas DD, Nikolovski Z, Nogues MV, Cuchillo CM, Acharya KR, Biochemistry. 1999 Dec 21;38(51):16794-801. PMID:10606511
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