2sh1 | pdb_00002sh1

SOLUTION STRUCTURE OF NEUROTOXIN I FROM THE SEA ANEMONE STICHODACTYLA HELIANTHUS. A NUCLEAR MAGNETIC RESONANCE, DISTANCE GEOMETRY AND RESTRAINED MOLECULAR DYNAMICS STUDY

spinqualitylabelsall models 2sh1, 8 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2sh1 is a 1 chain structure with sequence from Stichodactyla helianthus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1sh1 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The three-dimensional structure of the sea anemone polypeptide Stichodactyla helianthus neurotoxin I in aqueous solution has been determined using distance geometry and restrained molecular dynamics simulations based on NMR data acquired at 500 MHz. A set of 470 nuclear Overhauser enhancement values was measured, of which 216 were used as distance restraints in the structure determination along with 15 dihedral angles derived from coupling constants. After restrained molecular dynamics refinement, the eight structures that best fit the input data form a closely related family. They describe a structure that consists of a core of twisted, four-stranded, antiparallel beta-sheet encompassing residues 1-3, 19-24, 29-34, and 40-47, joined by three loops, two of which are well defined by the NMR data. The third loop, encompassing residues 7-16, is poorly defined by the data and is assumed to undergo conformational averaging in solution. Pairwise root mean square displacement values for the backbone heavy atoms of the eight best structures are 1.3 +/- 0.2A when the poorly defined loop is excluded and 3.6 +/- 1.0A for all backbone atoms. Refinement using restrained molecular dynamics improved the quality of the structures generated by distance geometry calculations with respect to the number of nuclear Overhauser enhancements violated, the size of the total distance violations and the total potential energies of the structures. The family of structures for S. heliathus neurotoxin I is compared with structures of related sea anemone proteins that also bind to the voltage-gated sodium channel. Solution structure of neurotoxin I from the sea anemone Stichodactyla helianthus. A nuclear magnetic resonance, distance geometry, and restrained molecular dynamics study.,Fogh RH, Kem WR, Norton RS J Biol Chem. 1990 Aug 5;265(22):13016-28. PMID:1973932 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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