1nxn
From Proteopedia
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|PDB= 1nxn |SIZE=350|CAPTION= <scene name='initialview01'>1nxn</scene> | |PDB= 1nxn |SIZE=350|CAPTION= <scene name='initialview01'>1nxn</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | + | |LIGAND= <scene name='pdbligand=DTR:D-TRYPTOPHAN'>DTR</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nxn OCA], [http://www.ebi.ac.uk/pdbsum/1nxn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nxn RCSB]</span> | ||
}} | }} | ||
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[[Category: Polticelli, F.]] | [[Category: Polticelli, F.]] | ||
[[Category: Schinina, M E.]] | [[Category: Schinina, M E.]] | ||
| - | [[Category: NH2]] | ||
[[Category: cis-trans isomerism]] | [[Category: cis-trans isomerism]] | ||
[[Category: cyclic peptide]] | [[Category: cyclic peptide]] | ||
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[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:36:55 2008'' |
Revision as of 19:36, 30 March 2008
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
1NXN is a Protein complex structure of sequences from [1]. 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
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