1qmt
From Proteopedia
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| - | [[Image:1qmt.gif|left|200px]] | + | [[Image:1qmt.gif|left|200px]] |
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| - | '''RECOMBINANT HUMAN EOSINOPHIL CATIONIC PROTEIN''' | + | {{Structure |
| + | |PDB= 1qmt |SIZE=350|CAPTION= <scene name='initialview01'>1qmt</scene>, resolution 2.40Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''RECOMBINANT HUMAN EOSINOPHIL CATIONIC PROTEIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QMT is a [ | + | 1QMT is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10606511 10606511] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ribonuclease]] | [[Category: ribonuclease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:39:52 2008'' |
Revision as of 11:39, 20 March 2008
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| , resolution 2.40Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
Page seeded by OCA on Thu Mar 20 13:39:52 2008
