1bon: Difference between revisions
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New page: left|200px<br /><applet load="1bon" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bon" /> '''THREE-DIMENSIONAL STRUCTURE OF BOMBYXIN-II, ... |
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[[Image:1bon.gif|left|200px]]<br /><applet load="1bon" size=" | [[Image:1bon.gif|left|200px]]<br /><applet load="1bon" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''THREE-DIMENSIONAL STRUCTURE OF BOMBYXIN-II, AN INSULIN-RELATED BRAIN-SECRETORY PEPTIDE OF THE SILKMOTH BOMBYX MORI: COMPARISON WITH INSULIN AND RELAXIN'''<br /> | '''THREE-DIMENSIONAL STRUCTURE OF BOMBYXIN-II, AN INSULIN-RELATED BRAIN-SECRETORY PEPTIDE OF THE SILKMOTH BOMBYX MORI: COMPARISON WITH INSULIN AND RELAXIN'''<br /> | ||
==Overview== | ==Overview== | ||
The three-dimensional solution structure of bombyxin-II, an insulin-like | 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. | ||
==About this Structure== | ==About this Structure== | ||
1BON is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http:// | 1BON is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BON OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Kohda, D.]] | [[Category: Kohda, D.]] | ||
[[Category: Nagata, K.]] | [[Category: Nagata, K.]] | ||
[[Category: SPINE, Structural | [[Category: SPINE, Structural Proteomics in Europe.]] | ||
[[Category: hormone]] | [[Category: hormone]] | ||
[[Category: spine]] | [[Category: spine]] | ||
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[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:57:29 2008'' | ||