1bom | pdb_00001bom

THREE-DIMENSIONAL STRUCTURE OF BOMBYXIN-II, AN INSULIN-RELATED BRAIN-SECRETORY PEPTIDE OF THE SILKMOTH BOMBYX MORI: COMPARISON WITH INSULIN AND RELAXIN

spinqualitylabelsall models 1bom, 1 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1bom is a 2 chain structure with sequence from Bommo. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: PCA Related: 1bon Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BXA2_BOMMO] Brain peptide responsible for activation of prothoracic glands to produce ecdysone in insects. [BXA6_BOMMO] Brain peptide responsible for activation of prothoracic glands to produce ecdysone in insects. Publication Abstract from PubMed The three-dimensional solution structure of bombyxin-II, an insulin-like two-chain peptide produced by the brain of the silkworm Bombyx mori, has been determined by simulated annealing calculations based on 535 distance constraints and 24 torsion-angle constraints derived from NMR data and three distance constraints of the disulfide bonds. To our knowledge, this is the first three-dimensional structure determined for an invertebrate insulin-related peptide. The root-mean-square deviations between the best 10 structures and the mean structure are 0.58(+/- 0.15) A for the backbone heavy atoms (N, C alpha, C) and 1.03(+/- 0.18) A for all non-hydrogen atom if less well-defined N and C termini (A1, A20, B(-2) to B4 and B23 to B25) are excluded. The overall main-chain structure of bombyxin-II is similar to that of insulin. However, there are significant conformational and functional differences in their B-chain C-terminal parts. The B-chain C-terminal part of bombyxin-II adopts an extension of the B-chain central helix like that of relaxin and is not required for bombyxin activity, while the corresponding part of insulin adopts a sharp turn and a beta-strand and is essential for insulin activity. This structure demonstrates that bombyxin-II is more closely related to relaxin than to insulin, and suggests that insulin might have evolved the additional receptor-recognition site in the B-chain C-terminal beta-strand to distinguish itself from bombyxin and relaxin. The structure of bombyxin-II thus provides novel insights into the receptor recognition and divergent molecular evolution of insulin-superfamily peptides. Three-dimensional solution structure of bombyxin-II an insulin-like peptide of the silkmoth Bombyx mori: structural comparison with insulin and relaxin.,Nagata K, Hatanaka H, Kohda D, Kataoka H, Nagasawa H, Isogai A, Ishizaki H, Suzuki A, Inagaki F J Mol Biol. 1995 Nov 10;253(5):749-58. PMID:7473749 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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