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1h1h

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[[Image:1h1h.gif|left|200px]]<br /><applet load="1h1h" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1h1h.gif|left|200px]]
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caption="1h1h, resolution 2.0&Aring;" />
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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'''<br />
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{{Structure
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|PDB= 1h1h |SIZE=350|CAPTION= <scene name='initialview01'>1h1h</scene>, resolution 2.0&Aring;
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|SITE= <scene name='pdbsite=A2P:A2p+Binding+Site+For+Chain+A'>A2P</scene>
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|LIGAND= <scene name='pdbligand=A2P:ADENOSINE-2'-5'-DIPHOSPHATE'>A2P</scene>
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|ACTIVITY=
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|GENE=
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}}
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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'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=A2P:'>A2P</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1H1H OCA].
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1H1H 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=1H1H OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12356310 12356310]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12356310 12356310]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: A2P]]
[[Category: A2P]]
[[Category: 5'-diphosphate]]
[[Category: 5'-diphosphate]]
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[[Category: adenosine-2']]
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[[Category: adenosine-2s']]
[[Category: eosinophil cationic protein]]
[[Category: eosinophil cationic protein]]
[[Category: eosinophil derived neurotoxin]]
[[Category: eosinophil derived neurotoxin]]
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[[Category: toxin]]
[[Category: toxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:56:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:30:51 2008''

Revision as of 09:30, 20 March 2008

Image:1h1h.gif


PDB ID 1h1h

Drag the structure with the mouse to rotate
, resolution 2.0Å
Sites:
Ligands:
Coordinates: save as pdb, mmCIF, xml



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


Overview

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 Structure

1H1H is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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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