1nxn
From Proteopedia
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[[Image:1nxn.gif|left|200px]] | [[Image:1nxn.gif|left|200px]] | ||
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'''SOLUTION STRUCTURE OF CONTRYPHAN-VN''' | '''SOLUTION STRUCTURE OF CONTRYPHAN-VN''' | ||
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==About this Structure== | ==About this Structure== | ||
- | + | This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1n3v 1n3v]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NXN OCA]. | |
==Reference== | ==Reference== | ||
Solution structure of the cyclic peptide contryphan-Vn, a Ca2+-dependent K+ channel modulator., Eliseo T, Cicero DO, Romeo C, Schinina ME, Massilia GR, Polticelli F, Ascenzi P, Paci M, Biopolymers. 2004 Jun 15;74(3):189-98. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15150794 15150794] | Solution structure of the cyclic peptide contryphan-Vn, a Ca2+-dependent K+ channel modulator., Eliseo T, Cicero DO, Romeo C, Schinina ME, Massilia GR, Polticelli F, Ascenzi P, Paci M, Biopolymers. 2004 Jun 15;74(3):189-98. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15150794 15150794] | ||
- | [[Category: Protein complex]] | ||
[[Category: Ascenzi, P.]] | [[Category: Ascenzi, P.]] | ||
[[Category: Cicero, D O.]] | [[Category: Cicero, D O.]] | ||
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[[Category: Polticelli, F.]] | [[Category: Polticelli, F.]] | ||
[[Category: Schinina, M E.]] | [[Category: Schinina, M E.]] | ||
- | [[Category: | + | [[Category: Cis-trans isomerism]] |
- | [[Category: | + | [[Category: Cyclic peptide]] |
- | [[Category: | + | [[Category: D-tryptophan]] |
- | [[Category: | + | [[Category: Disulfide bridge]] |
- | [[Category: | + | [[Category: Toxin]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:06:10 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 00:06, 3 May 2008
SOLUTION STRUCTURE OF CONTRYPHAN-VN
Overview
The solution structure of contryphan-Vn, a cyclic peptide with a double cysteine S-S bridge and containing a D-tryptophan extracted from the venom of the cone snail Conus ventricosus, has been determined by NMR spectroscopy using a variety of homonuclear and heteronuclear NMR methods and restrained molecular dynamics simulations. The main conformational features of backbone contryphan-Vn are a type IV beta-turn from Gly 1 to Lys 6 and a type I beta-turn from Lys 6 to Cys 9. As already found in other contryphans, one of the two prolines--the Pro4--is mainly in the cis conformation while Pro7 is trans. A small hydrophobic region probably partly shielded from solvent constituted from the close proximity of side chains of Pro7 and Trp8 was observed together with a persistent salt bridge between Asp2 and Lys6, which has been revealed by the diagnostic observation of specific nuclear Overhauser effects. The salt bridge was used as a restraint in the molecular dynamics in vacuum but without inserting explicit electrostatic contribution in the calculations. The backbone of the unique conformational family found of contryphan-Vn superimposes well with those of contryphan-Sm and contryphan-R. This result indicates that the contryphan structural motif represents a robust and conserved molecular scaffold whose main structural determinants are the size of the intercysteine loop and the presence and location in the sequence of the D-Trp and the two Pro residues.
About this Structure
This structure supersedes the now removed PDB entry 1n3v. Full crystallographic information is available from OCA.
Reference
Solution structure of the cyclic peptide contryphan-Vn, a Ca2+-dependent K+ channel modulator., Eliseo T, Cicero DO, Romeo C, Schinina ME, Massilia GR, Polticelli F, Ascenzi P, Paci M, Biopolymers. 2004 Jun 15;74(3):189-98. PMID:15150794 Page seeded by OCA on Sat May 3 03:06:10 2008