1bom: Difference between revisions

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[[Image:1bom.gif|left|200px]]<br /><applet load="1bom" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1bom.gif|left|200px]]<br /><applet load="1bom" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1bom" />

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

==Overview==

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.

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==

1BOM 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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1BOM OCA].

1BOM 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=1BOM OCA].

==Reference==

Line 19:

[[Category: insulin-like brain-secretory peptide]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 11:47:~~41 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:57:28 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1bom.gif|left|200px]]<br /><applet load="1bom" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1bom.gif|left|200px]]<br /><applet load="1bom" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1bom" />
 '''THREE-DIMENSIONAL STRUCTURE OF BOMBYXIN-II, AN INSULIN-RELATED BRAIN-SECRETORY PEPTIDE OF THE SILKMOTH BOMBYX MORI: COMPARISON WITH INSULIN AND RELAXIN'''<br />
 ==Overview==
-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.
+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==
-BOM 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BOM OCA].
+BOM 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=1BOM OCA].
 ==Reference==
@@ Line 19: / Line 19: @@
 [[Category: insulin-like brain-secretory peptide]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:47:41 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:57:28 2008''