1IRR
Solution structure of paralytic peptide of the silkworm, Bombyx mori
Summary for 1IRR
Entry DOI | 10.2210/pdb1irr/pdb |
NMR Information | BMRB: 5188 |
Descriptor | paralytic peptide (1 entity in total) |
Functional Keywords | single beta sheet, cytokine |
Total number of polymer chains | 1 |
Total formula weight | 2466.79 |
Authors | Miura, K.,Kamimura, M.,Aizawa, T.,Kiuchi, M.,Hayakawa, Y.,Mizuguchi, M.,Kawano, K. (deposition date: 2001-10-23, release date: 2003-02-11, Last modification date: 2024-10-30) |
Primary citation | Miura, K.,Kamimura, M.,Aizawa, T.,Kiuchi, M.,Hayakawa, Y.,Mizuguchi, M.,Kawano, K. Solution structure of paralytic peptide of silkworm, Bombyx mori peptides, 23:2111-2116, 2002 Cited by PubMed Abstract: 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. PubMed: 12535689DOI: 10.1016/S0196-9781(02)00254-1 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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