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1k2a

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|PDB= 1k2a |SIZE=350|CAPTION= <scene name='initialview01'>1k2a</scene>, resolution 1.00&Aring;
|PDB= 1k2a |SIZE=350|CAPTION= <scene name='initialview01'>1k2a</scene>, resolution 1.00&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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|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]
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|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=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k2a OCA], [http://www.ebi.ac.uk/pdbsum/1k2a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k2a RCSB]</span>
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==Overview==
==Overview==
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.
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.
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==Disease==
 
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Known disease associated with this structure: High density lipoprotein cholesterol level QTL 7 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=131240 131240]]
 
==About this Structure==
==About this Structure==
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[[Category: Rybak, S M.]]
[[Category: Rybak, S M.]]
[[Category: Wlodawer, A.]]
[[Category: Wlodawer, A.]]
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[[Category: SO4]]
 
[[Category: rnase a folding]]
[[Category: rnase a folding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:11:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:42:18 2008''

Revision as of 18:42, 30 March 2008


PDB ID 1k2a

Drag the structure with the mouse to rotate
, resolution 1.00Å
Ligands:
Activity: Pancreatic ribonuclease, with EC number 3.1.27.5
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Modified Form of Eosinophil-derived Neurotoxin


Overview

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.

About this Structure

1K2A is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

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