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.


1kbt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1kbt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kbt" /> '''SOLUTION STRUCTURE OF CARDIOTOXIN IV, NMR, 1...)
Current revision (07:59, 3 April 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1kbt.gif|left|200px]]<br /><applet load="1kbt" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1kbt" />
 
-
'''SOLUTION STRUCTURE OF CARDIOTOXIN IV, NMR, 12 STRUCTURES'''<br />
 
-
==Overview==
+
==SOLUTION STRUCTURE OF CARDIOTOXIN IV, NMR, 12 STRUCTURES==
-
Cardiotoxin analogues IV (CTX IV) and II (CTX II) isolated from the venom, of Taiwan Cobra (Naja naja atra) differ in their amino acid sequence by a, single amino acid at the N-terminal end. Leucine at the N-terminal end in, CTX II is replaced by arginine in CTX IV. CTX IV is an unique snake venom, cardiotoxin as it is the only cardiotoxin isoform known so far which, possesses a positively charged residue at the N-terminal amino acid. All, other cardiotoxins have a hydrophobic amino acid (leucine or isoleucine), at their N-terminal end. The aim of the present study is to understand the, effect(s) of the presence of a cationic residue on the structure and, functional properties of cardiotoxin(s). Comparison of the hemolytic, activities of CTX IV and CTX II shows that lytic activity of the former is, at least twice as that shown by the latter. Comparison of the solution, structures of CTX IV and CTX II using two-dimensional NMR spectroscopy and, dynamical simulated annealing technique reveals that the backbone fold of, both the toxin isoforms is almost similar. The secondary structural, elements in these two cardiotoxin isoforms consist of long, triple-stranded, as well as short, double-stranded, antiparallel, beta-sheets. Thermal denaturation experiments showed that the structure of, CTX IV is more stable than that of CTX II. Critical analysis of the, three-dimensional structures of CTX IV and CTX II reveals the presence of, a "cationic" cluster comprising of positively charged residues on the, concave side of the CTX IV molecule. Similar clusters consisting of, positively charged residues are not found in CTX II. The differential, erythrocyte lytic activities of these two cardiotoxins are attributed to, the difference(s) in the distribution of the positively charged residues, in their three-dimensional structures.
+
<StructureSection load='1kbt' size='340' side='right'caption='[[1kbt]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1kbt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KBT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KBT FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kbt OCA], [https://pdbe.org/1kbt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kbt RCSB], [https://www.ebi.ac.uk/pdbsum/1kbt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kbt ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/3SA4_NAJAT 3SA4_NAJAT] Basic protein that bind to cell membrane and depolarizes cardiomyocytes. This cytotoxin also shows lytic activities, but 2-fold more important than that of CTX-A2. It binds to the integrin alpha-V/beta-3 with a moderate affinity. Inhibits protein kinase C. It may interact with sulfatides in the cell membrane, which induces pore formation and cell internalization and is responsible for cytotoxicity in cardiomyocytes. It also may target the mitochondrial membrane and induces mitochondrial swelling and fragmentation.<ref>PMID:16407244</ref> <ref>PMID:8448165</ref> <ref>PMID:9398182</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kb/1kbt_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kbt ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1KBT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KBT OCA].
+
*[[Cardiotoxin 3D structures|Cardiotoxin 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
Comparison of the hemolytic activity and solution structures of two snake venom cardiotoxin analogues which only differ in their N-terminal amino acid., Jang JY, Krishnaswamy T, Kumar S, Jayaraman G, Yang PW, Yu C, Biochemistry. 1997 Dec 2;36(48):14635-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9398182 9398182]
+
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Naja atra]]
[[Category: Naja atra]]
-
[[Category: Single protein]]
+
[[Category: Jayaraman G]]
-
[[Category: Jayaraman, G.]]
+
[[Category: Jeng JY]]
-
[[Category: Jeng, J.Y.]]
+
[[Category: Kumar TKS]]
-
[[Category: Kumar, T.K.S.]]
+
[[Category: Yu C]]
-
[[Category: Yu, C.]]
+
-
[[Category: cardiotoxin]]
+
-
[[Category: cytotoxin]]
+
-
[[Category: multigene family]]
+
-
[[Category: venom]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:02:09 2007''
+

Current revision

SOLUTION STRUCTURE OF CARDIOTOXIN IV, NMR, 12 STRUCTURES

PDB ID 1kbt

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kbt"
Personal tools