2gvs

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(New page: 200px<br /><applet load="2gvs" size="350" color="white" frame="true" align="right" spinBox="true" caption="2gvs" /> '''NMR solution structure of CSPsg4'''<br /> =...)
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Revision as of 18:09, 29 January 2008


2gvs

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NMR solution structure of CSPsg4

Overview

Chemical stimuli, generally constituted by small volatile organic, molecules, are extremely important for the survival of different insect, species. In the course of evolution, insects have developed very, sophisticated biochemical systems for the binding and the delivery of, specific semiochemicals to their cognate membrane-bound receptors., Chemosensory proteins (CSPs) are a class of small soluble proteins present, at high concentration in insect chemosensory organs; they are supposed to, be involved in carrying the chemical messages from the environment to the, chemosensory receptors. In this paper, we report on the solution structure, of CSPsg4, a chemosensory protein from the desert locust Schistocerca, gregaria, which is expressed in the antennae and other chemosensory, organs. The 3D NMR structure revealed an overall fold consisting of six, alpha-helices, spanning residues 13-18, 20-31, 40-54, 62-78, 80-90, and, 97-103, connected by loops which in some cases show dihedral angles, typical of beta-turns. As in the only other chemosensory protein whose, structure has been solved so far, namely, CSP from the moth Mamestra, brassicae, four helices are arranged to form a V-shaped motif; another, helix runs across the two V's, and the last one is packed against the, external face. Analysis of the tertiary structure evidenced multiple, hydrophobic cavities which could be involved in ligand binding. In fact, incubation of the protein with a natural ligand, namely, oleamide, produced substantial changes to the NMR spectra, suggesting extensive, conformational transitions upon ligand binding.

About this Structure

2GVS is a Single protein structure of sequence from Schistocerca gregaria. Full crystallographic information is available from OCA.

Reference

Solution structure of a chemosensory protein from the desert locust Schistocerca gregaria., Tomaselli S, Crescenzi O, Sanfelice D, Ab E, Wechselberger R, Angeli S, Scaloni A, Boelens R, Tancredi T, Pelosi P, Picone D, Biochemistry. 2006 Sep 5;45(35):10606-13. PMID:16939212

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