1ter
From Proteopedia
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SOLUTION STRUCTURE OF TERTIAPIN DETERMINED USING NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY
Overview
The solution structure of tertiapin, a 21-residue bee venom peptide, has, been characterized by circular dichroism (CD), two-dimensional nuclear, magnetic resonance (NMR) spectroscopy, and distance geometry. A total of, 21 lowest error structures were obtained from distance geometry, calculations. Superimposition of these structures shows that the backbone, of tertiapin is very well defined. One type-I reverse turn from residue 4, to 7 and an alpha-helix from residue 12 to 19 exist in the structure of, tertiapin. The alpha-helical region is best defined from both, conformational analysis and structural superimposition. The overall, three-dimensional structure of tertiapin is highly compact resulting from, side chain interactions. The structural information obtained from CD and, NMR are compared for both tertiapin and apamin (ref. 3), another bee venom, peptide. Tertiapin and apamin have some similar secondary structure, but, display different tertiary structures.
About this Structure
1TER is a Single protein structure of sequence from Apis mellifera with NH2 as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of tertiapin determined using nuclear magnetic resonance and distance geometry., Xu X, Nelson JW, Proteins. 1993 Oct;17(2):124-37. PMID:8265561
Page seeded by OCA on Wed Nov 21 03:12:26 2007
Categories: Apis mellifera | Single protein | Nelson, J.W. | Xu, X. | NH2 | Toxin
