1lsi
From Proteopedia
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lsi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lsi OCA], [http://www.ebi.ac.uk/pdbsum/1lsi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lsi RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: venom]] | [[Category: venom]] | ||
| - | ''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 22:06:47 2008'' |
Revision as of 19:06, 30 March 2008
| |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
LSIII (NMR, 23 STRUCTURES)
Overview
We report the sequence-specific proton assignments and solution structure of the long neurotoxin LSIII from the venom of Laticauda semifasciata determined by two- and three-dimensional 1H NMR. Input for structure calculations consisted of 497 NOE-derived distance restraints and 45 dihedral angle restraints obtained from J couplings. A two-particle-per-residue representation of protein structure was used to generate 200 initial structures which were then subjected to all-atom refinement by simulated annealing. Twenty-three final structures consistent with the experimental restraints were obtained; the average atomic RMS difference between the individual structures and the mean structure was 0.82 A for the backbone heavy atoms and 1.3 A for all heavy atoms (residues 1-26, 37-60). The main elements of regular secondary structure are a three-stranded antiparallel beta-sheet and three finger-like loops protruding from a globular core, consistent with previously reported structures of long neurotoxins. The end of the prominent loop II, which is involved in binding to acetylcholine receptor, is disordered relative to the rest of the molecule. A novel finding of this study is that the loop has a well defined local structure; this and other observations suggest this region moves as a rigid body. We propose that this motion is a heretofore unrecognized general feature of long neurotoxins, with specific consequences for binding to the acetylcholine receptor.
About this Structure
1LSI is a Single protein structure of sequence from Laticauda semifasciata. Full crystallographic information is available from OCA.
Reference
Solution structure of LSIII, a long neurotoxin from the venom of Laticauda semifasciata., Connolly PJ, Stern AS, Hoch JC, Biochemistry. 1996 Jan 16;35(2):418-26. PMID:8555211
Page seeded by OCA on Sun Mar 30 22:06:47 2008
