2h4c: Difference between revisions

Revision as of 23:45, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2h4c.png

Template:STRUCTURE 2h4c

Structure of Daboiatoxin (heterodimeric PLA2 venom)Structure of Daboiatoxin (heterodimeric PLA2 venom)

Template:ABSTRACT PUBMED 17505111

About this StructureAbout this Structure

2H4C is a Protein complex structure of sequences from Daboia russellii siamensis. Full crystallographic information is available from OCA.

ReferenceReference

Structural and pharmacological comparison of daboiatoxin from Daboia russelli siamensis with viperotoxin F and vipoxin from other vipers., Gopalan G, Thwin MM, Gopalakrishnakone P, Swaminathan K, Acta Crystallogr D Biol Crystallogr. 2007 Jun;63(Pt 6):722-9. Epub 2007, May 15. PMID:17505111

Page seeded by OCA on Sun Jul 27 23:45:18 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2h4c.jpg|left|200px]]
+{{Seed}}
+[[Image:2h4c.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2h4c|  PDB=2h4c  |  SCENE=  }}
-'''Structure of Daboiatoxin (heterodimeric PLA2 venom)'''
+===Structure of Daboiatoxin (heterodimeric PLA2 venom)===
-==Overview==
+<!--
-Russell's viper (Vipera russelli, also known as Daboia russelli) is one of the major causes of fatal snakebites. To date, five Daboia russelli subspecies have been recognized. Daboiatoxin (DbTx) is the main lethal phospholipase A(2) (PLA(2)) toxin in the venom of D. russelli siamensis (Myanmar viper) and has strong neurotoxic, myotoxic and cytotoxic activities. DbTx and its homologous neurotoxins viperotoxin F from D. russelli formosensis (Taiwan viper) and vipoxin from the Bulgarian sand viper V. ammodytes meridionalis consist of complexes between a nontoxic acidic PLA(2) protein and an enzymatically active basic PLA(2). DbTx and viperotoxin F are presynaptic toxins, while vipoxin is postsynaptic. The two chains of DbTx have been separated and their PLA(2) enzymatic activity has been measured using the secretory PLA(2) assay kit. The enzymatic activity of DbTx chain B is reduced by 30% of its original activity by chain A in a unimolar ratio, thus indicating that DbTx chain A acts as an inhibitor. The lethal activity of the two chains has also been studied in male albino mice and chain A is less lethal than chain B. The crystal structure of DbTx has also been determined and its structural details are compared with those of the two homologues. Furthermore, an attempt is made to correlate the sequence and structural determinants of these toxins with their enzymatic activities and their pharmacological effects.
+The line below this paragraph, {{ABSTRACT_PUBMED_17505111}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17505111 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17505111}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Non-inhibitor acidic pla2]]
 [[Category: Phospholipase a2]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 05:51:10 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:45:18 2008''