1k2a: Difference between revisions
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==Modified Form of Eosinophil-derived Neurotoxin== | ==Modified Form of Eosinophil-derived Neurotoxin== | ||
<StructureSection load='1k2a' size='340' side='right' caption='[[1k2a]], [[Resolution|resolution]] 1.00Å' scene=''> | <StructureSection load='1k2a' size='340' side='right'caption='[[1k2a]], [[Resolution|resolution]] 1.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1k2a]] 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=1K2A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K2A FirstGlance]. <br> | <table><tr><td colspan='2'>[[1k2a]] 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=1K2A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K2A FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Pancreatic ribonuclease]] | [[Category: Pancreatic ribonuclease]] | ||
[[Category: Chang, C]] | [[Category: Chang, C]] | ||
Revision as of 12:00, 6 November 2019
Modified Form of Eosinophil-derived NeurotoxinModified Form 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 PubMedThe crystal structure of a post-translationally modified form of eosinophil-derived neurotoxin (EDN) with four extra residues on its N terminus ((-4)EDN) has been solved and refined at atomic resolution (1 A). Two of the extra residues can be placed unambiguously, while the density corresponding to two others is poor. The modified N terminus appears to influence the position of the catalytically important His129, possibly explaining the diminished catalytic activity of this variant. However, (-4)EDN has been shown to be cytotoxic to a Kaposi's sarcoma tumor cell line and other endothelial cell lines. Analysis of the structure and function suggests that the reason for cytotoxicity is most likely due to cellular recognition by the N-terminal extension, since the intrinsic activity of the enzyme is not sufficient for cytotoxicity and the N-terminal extension does not affect the conformation of EDN. Crystallographic and functional studies of a modified form of eosinophil-derived neurotoxin (EDN) with novel biological activities.,Chang C, Newton DL, Rybak SM, Wlodawer A J Mol Biol. 2002 Mar 15;317(1):119-30. PMID:11916383[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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