1ter | pdb_00001ter

SOLUTION STRUCTURE OF TERTIAPIN DETERMINED USING NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY

spinqualitylabelsall models 1ter, 21 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ter is a 1 chain structure with sequence from Apis mellifera. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: NH2 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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