1K2A
Modified Form of Eosinophil-derived Neurotoxin
Summary for 1K2A
| Entry DOI | 10.2210/pdb1k2a/pdb |
| Descriptor | eosinophil-derived neurotoxin, SULFATE ION (3 entities in total) |
| Functional Keywords | rnase a folding, hydrolase |
| Biological source | Homo sapiens (human) |
| Cellular location | Lysosome (Probable): P10153 |
| Total number of polymer chains | 1 |
| Total formula weight | 15909.96 |
| Authors | Chang, C.,Newton, D.L.,Rybak, S.M.,Wlodawer, A. (deposition date: 2001-09-26, release date: 2002-04-03, Last modification date: 2024-11-06) |
| Primary citation | Chang, C.,Newton, D.L.,Rybak, S.M.,Wlodawer, A. Crystallographic and functional studies of a modified form of eosinophil-derived neurotoxin (EDN) with novel biological activities. J.Mol.Biol., 317:119-130, 2002 Cited by PubMed Abstract: 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. PubMed: 11916383DOI: 10.1006/jmbi.2002.5406 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1 Å) |
Structure validation
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