1cvo

From Proteopedia

(Difference between revisions)

Revision as of 06:55, 10 October 2019

THE SOLUTION STRUCTURE OF CARDIOTOXIN V FROM NAJA NAJA ATRA

Structural highlights

1cvo is a 1 chain structure with sequence from Ansp 6988. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[3SOF5_NAJAT] Non-cytotoxic protein that does not show lytic and hemolytic activities, but can induce aggregation and fusion of sphingomyelin vesicles (PubMed:8182052). It binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with high affinity, and it inhibits osteoclast differentiation and bone resorption in mice, probably due to binding to integrin alpha-V/beta-3 (PubMed:16407244).^[1] ^[2] ^[3] ^[4]

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

Cardiotoxins are small proteins that are found in the venoms of snakes from the Elapidae family. These toxins are known to bind to and disrupt the organization, integrity, and function of the cell membrane. Most of the well-studied cardiotoxins cause depolarization of membrane potentials and/or lysis of red cells. In contrast, CTX V from Naja naja atra displays poor hemolytic activity but is proficient at inducing aggregation and fusion of sphingomyelin vesicles [Chien et al. (1991) J. Biol. Chem. 266, 3252-3259]. To determine whether the unique activity of this CTX is attributable to its tertiary structure, the solution structure of CTX V was determined by NMR methods. On the basis of these studies, this cardiotoxin has the same general topology as other members of the family, and thus its unusual properties do not arise from any gross structural differences that are detectable by solution NMR methods. Molecular dynamics calculations indicate that residues 36-50 show concerted fluctuations. On the basis of sequence similarity, we postulate that residues 30-34 are important in determining the specificity of cardiotoxins for fusion versus lysis of vesicles.

Solution structure of cardiotoxin V from Naja naja atra.,Singhal AK, Chien KY, Wu WG, Rule GS Biochemistry. 1993 Aug 10;32(31):8036-44. PMID:8347605^[5]

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

References

↑ Konshina AG, Volynskii PE, Arsen'ev AS, Efremov RG. [Interaction of cardiotoxin A5 with a membrane: role of conformational heterogeneity and hydrophilic properties] Bioorg Khim. 2003 Nov-Dec;29(6):577-88. PMID:14743531
↑ Wu PL, Lee SC, Chuang CC, Mori S, Akakura N, Wu WG, Takada Y. Non-cytotoxic cobra cardiotoxin A5 binds to alpha(v)beta3 integrin and inhibits bone resorption. Identification of cardiotoxins as non-RGD integrin-binding proteins of the Ly-6 family. J Biol Chem. 2006 Mar 24;281(12):7937-45. Epub 2006 Jan 10. PMID:16407244 doi:http://dx.doi.org/M513035200
↑ Chien KY, Chiang CM, Hseu YC, Vyas AA, Rule GS, Wu W. Two distinct types of cardiotoxin as revealed by the structure and activity relationship of their interaction with zwitterionic phospholipid dispersions. J Biol Chem. 1994 May 20;269(20):14473-83. PMID:8182052
↑ Chiang CM, Chien KY, Lin HJ, Lin JF, Yeh HC, Ho PL, Wu WG. Conformational change and inactivation of membrane phospholipid-related activity of cardiotoxin V from Taiwan cobra venom at acidic pH. Biochemistry. 1996 Jul 16;35(28):9167-76. PMID:8703922 doi:http://dx.doi.org/10.1021/bi952823k
↑ Singhal AK, Chien KY, Wu WG, Rule GS. Solution structure of cardiotoxin V from Naja naja atra. Biochemistry. 1993 Aug 10;32(31):8036-44. PMID:8347605

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/1cvo"

@@ Line 1: / Line 1: @@
 ==THE SOLUTION STRUCTURE OF CARDIOTOXIN V FROM NAJA NAJA ATRA==
-<StructureSection load='1cvo' size='340' side='right' caption='[[1cvo]], [[NMR_Ensembles_of_Models | 2 NMR models]]' scene=''>
+<StructureSection load='1cvo' size='340' side='right'caption='[[1cvo]], [[NMR_Ensembles_of_Models | 2 NMR models]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1cvo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ansp_6988 Ansp 6988]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CVO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CVO FirstGlance]. <br>
@@ Line 12: / Line 12: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cv/1cvo_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cv/1cvo_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 29: / Line 29: @@
 ==See Also==
+*[[Cardiotoxin 3D structures|Cardiotoxin 3D structures]]
 *[[NMR Ensembles of Models|NMR Ensembles of Models]]
 == References ==
@@ Line 35: / Line 36: @@
 </StructureSection>
 [[Category: Ansp 6988]]
+[[Category: Large Structures]]
 [[Category: Chien, K Y]]
 [[Category: Rule, G S]]

1cvo

From Proteopedia

Revision as of 06:55, 10 October 2019

THE SOLUTION STRUCTURE OF CARDIOTOXIN V FROM NAJA NAJA ATRA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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