1aok
From Proteopedia
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[[Image:1aok.gif|left|200px]] | [[Image:1aok.gif|left|200px]] | ||
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'''VIPOXIN COMPLEX''' | '''VIPOXIN COMPLEX''' | ||
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==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/9276469 9276469] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9276469 9276469] | ||
| - | [[Category: Phospholipase A(2)]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Vipera ammodytes meridionalis]] | [[Category: Vipera ammodytes meridionalis]] | ||
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[[Category: Perbandt, M.]] | [[Category: Perbandt, M.]] | ||
[[Category: Wilson, J C.]] | [[Category: Wilson, J C.]] | ||
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | [[Category: | + | [[Category: Phospholipase]] |
| - | [[Category: | + | [[Category: Pla2-activity]] |
| - | [[Category: | + | [[Category: Snake-venom]] |
| - | [[Category: | + | [[Category: Vipoxin]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:31:00 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:31, 2 May 2008
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. 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 Fri May 2 10:31:00 2008
