1aok
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1aok.gif|left|200px]] | + | [[Image:1aok.gif|left|200px]] |
| - | + | ||
| - | '''VIPOXIN COMPLEX''' | + | {{Structure |
| + | |PDB= 1aok |SIZE=350|CAPTION= <scene name='initialview01'>1aok</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''VIPOXIN COMPLEX''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1AOK is a [ | + | 1AOK is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Vipera_ammodytes_meridionalis Vipera ammodytes meridionalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOK OCA]. |
==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:// | + | 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: Phospholipase A(2)]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| Line 25: | Line 34: | ||
[[Category: vipoxin]] | [[Category: vipoxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:00:19 2008'' |
Revision as of 08:00, 20 March 2008
| |||||||
| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Phospholipase A(2), with EC number 3.1.1.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 10:00:19 2008
