1k2a: Difference between revisions

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New page: left|200px<br /> <applet load="1k2a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k2a, resolution 1.00Å" /> '''Modified Form of Eo...
 
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<applet load="1k2a" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1k2a, resolution 1.00&Aring;" />
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'''Modified Form of Eosinophil-derived Neurotoxin'''<br />
'''Modified Form of Eosinophil-derived Neurotoxin'''<br />


==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.


==Disease==
==Disease==
Known diseases associated with this structure: Central hypoventilation syndrome, congenital OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=131242 131242]], Hirschsprung disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=131242 131242]], Shah-Waardenburg syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=131242 131242]]
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==
1K2A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K2A OCA].  
1K2A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K2A OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Chang, C.]]
[[Category: Chang, C.]]
[[Category: Newton, D.L.]]
[[Category: Newton, D L.]]
[[Category: Rybak, S.M.]]
[[Category: Rybak, S M.]]
[[Category: Wlodawer, A.]]
[[Category: Wlodawer, A.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: rnase a folding]]
[[Category: rnase a folding]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:46:47 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:18 2008''

Revision as of 14:29, 21 February 2008

File:1k2a.gif


1k2a, resolution 1.00Å

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Modified Form of Eosinophil-derived Neurotoxin

OverviewOverview

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.

DiseaseDisease

Known disease associated with this structure: High density lipoprotein cholesterol level QTL 7 OMIM:[131240]

About this StructureAbout this Structure

1K2A is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Full crystallographic information is available from OCA.

ReferenceReference

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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