1h1h: Difference between revisions
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[[Image:1h1h.gif|left|200px]]<br /> | [[Image:1h1h.gif|left|200px]]<br /><applet load="1h1h" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1h1h" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1h1h, resolution 2.0Å" /> | caption="1h1h, resolution 2.0Å" /> | ||
'''CRYSTAL STRUCTURE OF EOSINOPHIL CATIONIC PROTEIN IN COMPLEX WITH 2',5'-ADP AT 2.0 A RESOLUTION REVEALS THE DETAILS OF THE RIBONUCLEOLYTIC ACTIVE SITE'''<br /> | '''CRYSTAL STRUCTURE OF EOSINOPHIL CATIONIC PROTEIN IN COMPLEX WITH 2',5'-ADP AT 2.0 A RESOLUTION REVEALS THE DETAILS OF THE RIBONUCLEOLYTIC ACTIVE SITE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1H1H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with A2P as [http://en.wikipedia.org/wiki/ligand ligand]. | 1H1H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with A2P as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=A2P:A2p Binding Site For Chain A'>A2P</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H1H OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: toxin]] | [[Category: toxin]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:52:14 2007'' | ||
Revision as of 16:42, 18 December 2007
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CRYSTAL STRUCTURE OF EOSINOPHIL CATIONIC PROTEIN IN COMPLEX WITH 2',5'-ADP AT 2.0 A RESOLUTION REVEALS THE DETAILS OF THE RIBONUCLEOLYTIC ACTIVE SITE
OverviewOverview
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 A) 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 P(1), site, while His-128 interacts with the purine ring at the B(2) 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.
About this StructureAbout this Structure
1H1H is a Single protein structure of sequence from Homo sapiens with A2P as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of eosinophil cationic protein in complex with 2',5'-ADP at 2.0 A resolution reveals the details of the ribonucleolytic active site., Mohan CG, Boix E, Evans HR, Nikolovski Z, Nogues MV, Cuchillo CM, Acharya KR, Biochemistry. 2002 Oct 8;41(40):12100-6. PMID:12356310
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