1kbt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1kbt.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1kbt.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1kbt| PDB=1kbt | SCENE= }}
{{STRUCTURE_1kbt| PDB=1kbt | SCENE= }}
-
'''SOLUTION STRUCTURE OF CARDIOTOXIN IV, NMR, 12 STRUCTURES'''
+
===SOLUTION STRUCTURE OF CARDIOTOXIN IV, NMR, 12 STRUCTURES===
-
==Overview==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9398182}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9398182 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9398182}}
==About this Structure==
==About this Structure==
-
1KBT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KBT OCA].
+
1KBT is a [[Single protein]] structure of sequence from [http://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].
==Reference==
==Reference==
Line 30: Line 34:
[[Category: Multigene family]]
[[Category: Multigene family]]
[[Category: Venom]]
[[Category: Venom]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:33:12 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:06:00 2008''

Revision as of 07:06, 2 July 2008

Image:1kbt.png

Template:STRUCTURE 1kbt

SOLUTION STRUCTURE OF CARDIOTOXIN IV, NMR, 12 STRUCTURES

Template:ABSTRACT PUBMED 9398182

About this Structure

1KBT is a Single protein structure of sequence from Naja atra. Full experimental information is available from OCA.

Reference

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:9398182

Page seeded by OCA on Wed Jul 2 10:06:00 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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