ISDA: 1IRR

Deposition Date 2001-10-23

Release Date 2003-02-11

Last Version Date 2024-10-30

Entry Detail

PDB ID:

1IRR

Keywords:

CYTOKINE

Title:

Solution structure of paralytic peptide of the silkworm, Bombyx mori

Method Details:

Experimental Method:

SOLUTION NMR

Conformers Calculated:

100

Conformers Submitted:

Selection Criteria:

structures with the lowest energy

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Macromolecular Entities

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:paralytic peptide
Gene (Uniprot):BmPP
Chain IDs:A
Chain Length:23
Number of Molecules:1
Biological Source:

UniProt ID:Q95YI2 Pfam ID:PF02425

Ligand Molecules

Primary Citation

Solution structure of paralytic peptide of silkworm, Bombyx mori

Miura, K, Kamimura, M, Aizawa, T, Kiuchi, M, Hayakawa, Y, Mizuguchi, M, Kawano, K.Show

Peptides 23 2111 2116 (2002)

PMID: 12535689 DOI: 10.1016/S0196-9781(02)00254-1

Abstact

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.

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Protein

Chemical

Disease

Primary Citation of related structures

Abstact

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