1bon: Difference between revisions

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[[Image:1bon.gif|left|200px]]
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{{STRUCTURE_1bon|  PDB=1bon  |  SCENE=  }}  
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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'''
===THREE-DIMENSIONAL STRUCTURE OF BOMBYXIN-II, AN INSULIN-RELATED BRAIN-SECRETORY PEPTIDE OF THE SILKMOTH BOMBYX MORI: COMPARISON WITH INSULIN AND RELAXIN===




==Overview==
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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.
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{{ABSTRACT_PUBMED_7473749}}


==About this Structure==
==About this Structure==
1BON is a [[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].  
1BON is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BON OCA].  


==Reference==
==Reference==
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Structural proteomics in europe]]
[[Category: Structural proteomics in europe]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:05:45 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:27:59 2008''

Revision as of 16:28, 30 June 2008

File:1bon.png

Template:STRUCTURE 1bon

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

Template:ABSTRACT PUBMED 7473749

About this Structure

1BON is a Protein complex structure of sequences from Bombyx mori. Full experimental information is available from OCA.

Reference

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

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