1irr

Solution structure of paralytic peptide of the silkworm, Bombyx mori

spinqualitylabelsall models 1irr Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1irr is a 1 chain structure with sequence from Bombyx mori. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q95YI2_BOMMO Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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