1aok
From Proteopedia
|  (New page: 200px<br /><applet load="1aok" size="450" color="white" frame="true" align="right" spinBox="true"  caption="1aok, resolution 2.0Å" /> '''VIPOXIN COMPLEX'''<br...) | |||
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| - | [[Image:1aok.gif|left|200px]]<br /><applet load="1aok" size=" | + | [[Image:1aok.gif|left|200px]]<br /><applet load="1aok" size="350" color="white" frame="true" align="right" spinBox="true"  | 
| caption="1aok, resolution 2.0Å" /> | caption="1aok, resolution 2.0Å" /> | ||
| '''VIPOXIN COMPLEX'''<br /> | '''VIPOXIN COMPLEX'''<br /> | ||
| ==Overview== | ==Overview== | ||
| - | Vipoxin is the main toxic component in the venom of the Bulgarian snake | + | Vipoxin is the main toxic component in the venom of the Bulgarian snake Vipera ammodytes meridionalis, the most toxic snake in Europe. Vipoxin is a complex between a toxic phospholipase A2 (PLA2) and a non-toxic protein inhibitor. The structure is of genetic interest due to the high degree of sequence homology (62%) between the two functionally different components. The structure shows that the formation of the complex in vipoxin is significantly different to that seen in many known structures of phospholipases and contradicts the assumptions made in earlier studies. The modulation of PLA2 activity is of great pharmacological interest, and the present structure will be a model for structure-based drug design. | 
| ==About this Structure== | ==About this Structure== | ||
| - | 1AOK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Vipera_ammodytes_meridionalis Vipera ammodytes meridionalis] with ACT as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] Full crystallographic information is available from [http:// | + | 1AOK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Vipera_ammodytes_meridionalis Vipera ammodytes meridionalis] with <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOK OCA].  | 
| ==Reference== | ==Reference== | ||
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| [[Category: Eschenburg, S.]] | [[Category: Eschenburg, S.]] | ||
| [[Category: Perbandt, M.]] | [[Category: Perbandt, M.]] | ||
| - | [[Category: Wilson, J | + | [[Category: Wilson, J C.]] | 
| [[Category: ACT]] | [[Category: ACT]] | ||
| [[Category: hydrolase]] | [[Category: hydrolase]] | ||
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| [[Category: vipoxin]] | [[Category: vipoxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:41 2008'' | 
Revision as of 09:46, 21 February 2008
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VIPOXIN COMPLEX
Overview
Vipoxin is the main toxic component in the venom of the Bulgarian snake Vipera ammodytes meridionalis, the most toxic snake in Europe. Vipoxin is a complex between a toxic phospholipase A2 (PLA2) and a non-toxic protein inhibitor. The structure is of genetic interest due to the high degree of sequence homology (62%) between the two functionally different components. The structure shows that the formation of the complex in vipoxin is significantly different to that seen in many known structures of phospholipases and contradicts the assumptions made in earlier studies. The modulation of PLA2 activity is of great pharmacological interest, and the present structure will be a model for structure-based drug design.
About this Structure
1AOK is a Protein complex structure of sequences from Vipera ammodytes meridionalis with as ligand. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.
Reference
Crystal structure of vipoxin at 2.0 A: an example of regulation of a toxic function generated by molecular evolution., Perbandt M, Wilson JC, Eschenburg S, Mancheva I, Aleksiev B, Genov N, Willingmann P, Weber W, Singh TP, Betzel C, FEBS Lett. 1997 Aug 4;412(3):573-7. PMID:9276469
Page seeded by OCA on Thu Feb 21 11:46:41 2008
