1gqv: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
==Atomic Resolution (0.98A) Structure of Eosinophil-Derived Neurotoxin== | ==Atomic Resolution (0.98A) Structure of Eosinophil-Derived Neurotoxin== | ||
<StructureSection load='1gqv' size='340' side='right' caption='[[1gqv]], [[Resolution|resolution]] 0.98Å' scene=''> | <StructureSection load='1gqv' size='340' side='right'caption='[[1gqv]], [[Resolution|resolution]] 0.98Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1gqv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GQV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GQV FirstGlance]. <br> | <table><tr><td colspan='2'>[[1gqv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GQV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GQV FirstGlance]. <br> | ||
Line 35: | Line 35: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Pancreatic ribonuclease]] | [[Category: Pancreatic ribonuclease]] | ||
[[Category: Acharya, K R]] | [[Category: Acharya, K R]] |
Revision as of 10:01, 23 May 2019
Atomic Resolution (0.98A) Structure of Eosinophil-Derived NeurotoxinAtomic Resolution (0.98A) Structure of Eosinophil-Derived Neurotoxin
Structural highlights
Function[RNAS2_HUMAN] This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Selectively chemotactic for dendritic cells. Possesses a wide variety of biological activities.[1] [2] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHuman 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. 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
|