1bqf

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(New page: 200px<br /><applet load="1bqf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bqf" /> '''GROWTH-BLOCKING PEPTIDE (GBP) FROM PSEUDALET...)
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'''GROWTH-BLOCKING PEPTIDE (GBP) FROM PSEUDALETIA SEPARATA'''<br />
'''GROWTH-BLOCKING PEPTIDE (GBP) FROM PSEUDALETIA SEPARATA'''<br />
==Overview==
==Overview==
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Growth-blocking peptide (GBP) is an insect growth factor consisting of 25, amino acid residues that retards the development of lepidopteran larvae at, high concentration while it stimulates larval growth at low concentration., In this study, we determined the solution structure of GBP by, two-dimensional 1H NMR spectroscopy. The structure contains a short, segment of double-stranded beta-sheet involving residues 11-13 and 19-21, and a type-II beta-turn in the loop region (residues 8-11), whereas the N, and C termini are disordered. This is the first report of the, three-dimensional structure of the peptiderigic insect growth factor, and, the structure of the well defined region of GBP was found to share, similarity with that of the C-terminal domain of the epidermal growth, factor (EGF). Because GBP has been reported to stimulate DNA synthesis of, not only insect cells but also human keratinocyte cells at the same level, with EGF, the structural similarity between GBP and EGF may lead to the, interaction of GBP to EGF receptor.
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Growth-blocking peptide (GBP) is an insect growth factor consisting of 25 amino acid residues that retards the development of lepidopteran larvae at high concentration while it stimulates larval growth at low concentration. In this study, we determined the solution structure of GBP by two-dimensional 1H NMR spectroscopy. The structure contains a short segment of double-stranded beta-sheet involving residues 11-13 and 19-21 and a type-II beta-turn in the loop region (residues 8-11), whereas the N and C termini are disordered. This is the first report of the three-dimensional structure of the peptiderigic insect growth factor, and the structure of the well defined region of GBP was found to share similarity with that of the C-terminal domain of the epidermal growth factor (EGF). Because GBP has been reported to stimulate DNA synthesis of not only insect cells but also human keratinocyte cells at the same level with EGF, the structural similarity between GBP and EGF may lead to the interaction of GBP to EGF receptor.
==About this Structure==
==About this Structure==
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1BQF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Apanteles_kariyai Apanteles kariyai]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BQF OCA].
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1BQF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Apanteles_kariyai Apanteles kariyai]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BQF OCA].
==Reference==
==Reference==
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[[Category: growth factor]]
[[Category: growth factor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:50:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:00 2008''

Revision as of 09:58, 21 February 2008


1bqf

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GROWTH-BLOCKING PEPTIDE (GBP) FROM PSEUDALETIA SEPARATA

Overview

Growth-blocking peptide (GBP) is an insect growth factor consisting of 25 amino acid residues that retards the development of lepidopteran larvae at high concentration while it stimulates larval growth at low concentration. In this study, we determined the solution structure of GBP by two-dimensional 1H NMR spectroscopy. The structure contains a short segment of double-stranded beta-sheet involving residues 11-13 and 19-21 and a type-II beta-turn in the loop region (residues 8-11), whereas the N and C termini are disordered. This is the first report of the three-dimensional structure of the peptiderigic insect growth factor, and the structure of the well defined region of GBP was found to share similarity with that of the C-terminal domain of the epidermal growth factor (EGF). Because GBP has been reported to stimulate DNA synthesis of not only insect cells but also human keratinocyte cells at the same level with EGF, the structural similarity between GBP and EGF may lead to the interaction of GBP to EGF receptor.

About this Structure

1BQF is a Single protein structure of sequence from Apanteles kariyai. Full crystallographic information is available from OCA.

Reference

Solution structure of an insect growth factor, growth-blocking peptide., Aizawa T, Fujitani N, Hayakawa Y, Ohnishi A, Ohkubo T, Kumaki Y, Kawano K, Hikichi K, Nitta K, J Biol Chem. 1999 Jan 22;274(4):1887-90. PMID:9890941

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