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1irr
From Proteopedia
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(New page: 200px<br /><applet load="1irr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1irr" /> '''Solution structure of paralytic peptide of t...)
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Revision as of 20:18, 24 November 2007
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Solution structure of paralytic peptide of the silkworm, Bombyx mori
Overview
Paralytic peptide of Bombyx mori (BmPP) is one of the multifunctional, ENF-peptides; the name of "ENF" is the consensus N-terminal amino acid, sequence of the family peptides. We revealed that BmPP significantly, possesses growth-blocking activity and plasmatocyte-spreading activity and, that its activity profiles are different from those of another ENF-family, peptide, namely, the growth-blocking peptide of Pseudaletia separata, (PsGBP). We also determined the NMR structures of BmPP and PsGBP under the, same conditions, which revealed the structural differences of the first, and second beta-turn regions between the two peptides. On the basis of our, results, it can be considered that the tertiary structural difference in, these peptides may cause their different profiles of growth-blocking, activity.
About this Structure
1IRR is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Solution structure of paralytic peptide of silkworm, Bombyx mori., Miura K, Kamimura M, Aizawa T, Kiuchi M, Hayakawa Y, Mizuguchi M, Kawano K, Peptides. 2002 Dec;23(12):2111-6. PMID:12535689
Page seeded by OCA on Sat Nov 24 22:26:09 2007
