1b1v

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(New page: 200px<br /><applet load="1b1v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b1v" /> '''NMR STRUCTURE OF PSP1, PLASMATOCYTE-SPREADIN...)
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'''NMR STRUCTURE OF PSP1, PLASMATOCYTE-SPREADING PEPTIDE FROM PSEUDOPLUSIA INCLUDENS'''<br />
'''NMR STRUCTURE OF PSP1, PLASMATOCYTE-SPREADING PEPTIDE FROM PSEUDOPLUSIA INCLUDENS'''<br />
==Overview==
==Overview==
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The structure of the recently identified plasmatocyte spreading peptide, from the moth Pseudoplusia includens (PSP1) has been determined by NMR, spectroscopy. This novel insect cytokine consists of 23 amino acid, residues and a single disulfide bond. Torsion angle dynamics calculations, utilizing a total of 337 distance constraints yielded an ensemble of 30, structures with an average backbone root mean square deviation for, residues 7-22 of 0.18 A from the mean structure. The structure consists of, a disordered N-terminal region and a well defined core that is stabilized, by numerous hydrophobic interactions and a short beta-hairpin. Structural, comparisons confirm that PSP1 adopts an epidermal growth factor (EGF)-like, fold with close similarity to the C-terminal subdomain of EGF-like module, 5 of human thrombomodulin. The combination of the three-dimensional, structure of PSP1 and the extensive literature on EGF-receptor, interactions should accelerate the process of identifying the specific, residues responsible for receptor binding activity of this family of, immunoregulatory peptides.
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The structure of the recently identified plasmatocyte spreading peptide from the moth Pseudoplusia includens (PSP1) has been determined by NMR spectroscopy. This novel insect cytokine consists of 23 amino acid residues and a single disulfide bond. Torsion angle dynamics calculations utilizing a total of 337 distance constraints yielded an ensemble of 30 structures with an average backbone root mean square deviation for residues 7-22 of 0.18 A from the mean structure. The structure consists of a disordered N-terminal region and a well defined core that is stabilized by numerous hydrophobic interactions and a short beta-hairpin. Structural comparisons confirm that PSP1 adopts an epidermal growth factor (EGF)-like fold with close similarity to the C-terminal subdomain of EGF-like module 5 of human thrombomodulin. The combination of the three-dimensional structure of PSP1 and the extensive literature on EGF-receptor interactions should accelerate the process of identifying the specific residues responsible for receptor binding activity of this family of immunoregulatory peptides.
==About this Structure==
==About this Structure==
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1B1V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B1V OCA].
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1B1V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B1V OCA].
==Reference==
==Reference==
Structure of the insect cytokine peptide plasmatocyte-spreading peptide 1 from Pseudoplusia includens., Volkman BF, Anderson ME, Clark KD, Hayakawa Y, Strand MR, Markley JL, J Biol Chem. 1999 Feb 19;274(8):4493-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9988679 9988679]
Structure of the insect cytokine peptide plasmatocyte-spreading peptide 1 from Pseudoplusia includens., Volkman BF, Anderson ME, Clark KD, Hayakawa Y, Strand MR, Markley JL, J Biol Chem. 1999 Feb 19;274(8):4493-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9988679 9988679]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Anderson, M.E.]]
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[[Category: Anderson, M E.]]
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[[Category: Clark, K.D.]]
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[[Category: Clark, K D.]]
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[[Category: Markley, J.L.]]
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[[Category: Markley, J L.]]
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[[Category: Pech, L.L.]]
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[[Category: Pech, L L.]]
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[[Category: Strand, M.R.]]
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[[Category: Strand, M R.]]
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[[Category: Volkman, B.F.]]
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[[Category: Volkman, B F.]]
[[Category: egf-like]]
[[Category: egf-like]]
[[Category: insect cytokine]]
[[Category: insect cytokine]]
[[Category: plasmatocyte-spreading]]
[[Category: plasmatocyte-spreading]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:17:03 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:50:33 2008''

Revision as of 09:50, 21 February 2008


1b1v

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NMR STRUCTURE OF PSP1, PLASMATOCYTE-SPREADING PEPTIDE FROM PSEUDOPLUSIA INCLUDENS

Overview

The structure of the recently identified plasmatocyte spreading peptide from the moth Pseudoplusia includens (PSP1) has been determined by NMR spectroscopy. This novel insect cytokine consists of 23 amino acid residues and a single disulfide bond. Torsion angle dynamics calculations utilizing a total of 337 distance constraints yielded an ensemble of 30 structures with an average backbone root mean square deviation for residues 7-22 of 0.18 A from the mean structure. The structure consists of a disordered N-terminal region and a well defined core that is stabilized by numerous hydrophobic interactions and a short beta-hairpin. Structural comparisons confirm that PSP1 adopts an epidermal growth factor (EGF)-like fold with close similarity to the C-terminal subdomain of EGF-like module 5 of human thrombomodulin. The combination of the three-dimensional structure of PSP1 and the extensive literature on EGF-receptor interactions should accelerate the process of identifying the specific residues responsible for receptor binding activity of this family of immunoregulatory peptides.

About this Structure

1B1V is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

Structure of the insect cytokine peptide plasmatocyte-spreading peptide 1 from Pseudoplusia includens., Volkman BF, Anderson ME, Clark KD, Hayakawa Y, Strand MR, Markley JL, J Biol Chem. 1999 Feb 19;274(8):4493-6. PMID:9988679

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