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 2.40&Aring;" /> '''RECOMBINANT HUMAN E...)
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caption="1qmt, resolution 2.40&Aring;" />
'''RECOMBINANT HUMAN EOSINOPHIL CATIONIC PROTEIN'''<br />
'''RECOMBINANT HUMAN EOSINOPHIL CATIONIC PROTEIN'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1QMT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QMT OCA].
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1QMT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QMT OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Acharya, K.R.]]
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[[Category: Acharya, K R.]]
[[Category: Boix, E.]]
[[Category: Boix, E.]]
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[[Category: Leonidas, D.D.]]
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[[Category: Leonidas, D D.]]
[[Category: cytotoxicity]]
[[Category: cytotoxicity]]
[[Category: eosinophil]]
[[Category: eosinophil]]
[[Category: ribonuclease]]
[[Category: ribonuclease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:54:50 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:41:24 2008''

Revision as of 12:41, 21 February 2008


1qmt, resolution 2.40Å

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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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