1k2a: Difference between revisions

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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1k2a ConSurf].
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Revision as of 17:09, 7 February 2016

Modified Form of Eosinophil-derived NeurotoxinModified Form of Eosinophil-derived Neurotoxin

Structural highlights

1k2a is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:Pancreatic ribonuclease, with EC number 3.1.27.5
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

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 PubMed

The 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

  1. Gleich GJ, Loegering DA, Bell MP, Checkel JL, Ackerman SJ, McKean DJ. Biochemical and functional similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein: homology with ribonuclease. Proc Natl Acad Sci U S A. 1986 May;83(10):3146-50. PMID:3458170
  2. Teufel DP, Kao RY, Acharya KR, Shapiro R. Mutational analysis of the complex of human RNase inhibitor and human eosinophil-derived neurotoxin (RNase 2). Biochemistry. 2003 Feb 18;42(6):1451-9. PMID:12578357 doi:10.1021/bi026852o
  3. Chang C, Newton DL, Rybak SM, Wlodawer A. Crystallographic and functional studies of a modified form of eosinophil-derived neurotoxin (EDN) with novel biological activities. J Mol Biol. 2002 Mar 15;317(1):119-30. PMID:11916383 doi:http://dx.doi.org/10.1006/jmbi.2002.5406

1k2a, resolution 1.00Å

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OCA