This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2h4c

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 10:05, 1 April 2020

Structure of Daboiatoxin (heterodimeric PLA2 venom)

Structural highlights

2h4c is a 8 chain structure with sequence from Daboia russellii siamensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Phospholipase A(2), with EC number 3.1.1.4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PA2AA_DABSI] Heterodimer (A and B chains): phospholipase A2 that acts as a presynaptic neurotoxin and shows a PLA2 activity of 1377 umol/min/mg. In vivo, induces edema and produces neurotoxic symptoms in mice. Also exhibits indirect hemolysis, a strong myonecrotic activity and cytotoxicity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Monomer: Snake venom phospholipase A2 (PLA2) that shows a PLA2 activity of 578 umol/min/mg. [PA2AB_DABSI] Monomer: Snake venom phospholipase A2 (PLA2) that shows a high PLA2 activity (2110 umol/min/mg). Heterodimer (A and B chains): snake venom phospholipase A2 that shows a moderate PLA2 activity (1377 umol/min/mg). Acts as a presynaptic neurotoxin. In vivo, induces edema and produces neurotoxic symptoms in mice. It exhibits indirect hemolysis and a strong myonecrotic activity and is cytotoxic. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gopalan G, Thwin MM, Gopalakrishnakone P, Swaminathan K. Structural and pharmacological comparison of daboiatoxin from Daboia russelli siamensis with viperotoxin F and vipoxin from other vipers. Acta Crystallogr D Biol Crystallogr. 2007 Jun;63(Pt 6):722-9. Epub 2007, May 15. PMID:17505111 doi:10.1107/S0907444907016204

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2h4c"

@@ Line 1: / Line 1: @@
 ==Structure of Daboiatoxin (heterodimeric PLA2 venom)==
-<StructureSection load='2h4c' size='340' side='right' caption='[[2h4c]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+<StructureSection load='2h4c' size='340' side='right'caption='[[2h4c]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2h4c]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Daboia_russellii_siamensis Daboia russellii siamensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H4C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H4C FirstGlance]. <br>
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Phospholipase A2|Phospholipase A2]]
+*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
 == References ==
 <references/>
@@ Line 36: / Line 36: @@
 </StructureSection>
 [[Category: Daboia russellii siamensis]]
+[[Category: Large Structures]]
 [[Category: Gopalakrishnakone, P]]
 [[Category: Gopalan, G]]

2h4c

From Proteopedia

Revision as of 10:05, 1 April 2020

Structure of Daboiatoxin (heterodimeric PLA2 venom)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox