1gqv: Difference between revisions
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|PDB= 1gqv |SIZE=350|CAPTION= <scene name='initialview01'>1gqv</scene>, resolution 0.98Å | |PDB= 1gqv |SIZE=350|CAPTION= <scene name='initialview01'>1gqv</scene>, resolution 0.98Å | ||
|SITE= <scene name='pdbsite=AC1:P-1+Peripheral+Subsite+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:P-1+Peripheral+Subsite+For+Chain+A'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene> | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gqv OCA], [http://www.ebi.ac.uk/pdbsum/1gqv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gqv RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
Human eosinophil-derived neurotoxin (EDN) is a small, basic protein that belongs to the ribonuclease A superfamily. EDN displays antiviral activity and causes the neurotoxic Gordon phenomenon when injected into rabbits. Although EDN and ribonuclease A have appreciable structural similarity and a conserved catalytic triad, their peripheral substrate-binding sites are not conserved. The crystal structure of recombinant EDN (rEDN) has been determined at 0.98 A resolution from data collected at a low temperature (100 K). We have refined the crystallographic model of the structure using anisotropic displacement parameters to a conventional R-factor of 0.116. This represents the highest resolution structure of rEDN determined to date and is only the second ribonuclease structure to be determined at a resolution greater than 1.0 A. The structure provides a detailed picture of the conformational freedom at the various subsites of rEDN, and the water structure accounts for more than 50% of the total solvent content of the unit cell. This information will be crucial for the design of tight-binding inhibitors to restrain the ribonucleolytic activity of rEDN. | Human eosinophil-derived neurotoxin (EDN) is a small, basic protein that belongs to the ribonuclease A superfamily. EDN displays antiviral activity and causes the neurotoxic Gordon phenomenon when injected into rabbits. Although EDN and ribonuclease A have appreciable structural similarity and a conserved catalytic triad, their peripheral substrate-binding sites are not conserved. The crystal structure of recombinant EDN (rEDN) has been determined at 0.98 A resolution from data collected at a low temperature (100 K). We have refined the crystallographic model of the structure using anisotropic displacement parameters to a conventional R-factor of 0.116. This represents the highest resolution structure of rEDN determined to date and is only the second ribonuclease structure to be determined at a resolution greater than 1.0 A. The structure provides a detailed picture of the conformational freedom at the various subsites of rEDN, and the water structure accounts for more than 50% of the total solvent content of the unit cell. This information will be crucial for the design of tight-binding inhibitors to restrain the ribonucleolytic activity of rEDN. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Swaminathan, G J.]] | [[Category: Swaminathan, G J.]] | ||
[[Category: Veluraja, K.]] | [[Category: Veluraja, K.]] | ||
[[Category: ribonuclease]] | [[Category: ribonuclease]] | ||
[[Category: rnase us]] | [[Category: rnase us]] | ||
[[Category: rnase-2]] | [[Category: rnase-2]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:49:43 2008'' | ||
Revision as of 20:49, 30 March 2008
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| , resolution 0.98Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Pancreatic ribonuclease, with EC number 3.1.27.5 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ATOMIC RESOLUTION (0.98A) STRUCTURE OF EOSINOPHIL-DERIVED NEUROTOXIN
OverviewOverview
Human eosinophil-derived neurotoxin (EDN) is a small, basic protein that belongs to the ribonuclease A superfamily. EDN displays antiviral activity and causes the neurotoxic Gordon phenomenon when injected into rabbits. Although EDN and ribonuclease A have appreciable structural similarity and a conserved catalytic triad, their peripheral substrate-binding sites are not conserved. The crystal structure of recombinant EDN (rEDN) has been determined at 0.98 A resolution from data collected at a low temperature (100 K). We have refined the crystallographic model of the structure using anisotropic displacement parameters to a conventional R-factor of 0.116. This represents the highest resolution structure of rEDN determined to date and is only the second ribonuclease structure to be determined at a resolution greater than 1.0 A. The structure provides a detailed picture of the conformational freedom at the various subsites of rEDN, and the water structure accounts for more than 50% of the total solvent content of the unit cell. This information will be crucial for the design of tight-binding inhibitors to restrain the ribonucleolytic activity of rEDN.
About this StructureAbout this Structure
1GQV is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Atomic resolution (0.98 A) structure of eosinophil-derived neurotoxin., Swaminathan GJ, Holloway DE, Veluraja K, Acharya KR, Biochemistry. 2002 Mar 12;41(10):3341-52. PMID:11876642
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