Faculty Collaboration Database

Structure of the insect cytokine peptide plasmatocyte-spreading peptide 1 from Pseudoplusia includens. J Biol Chem 1999 Feb 19;274(8):4493-6

Date

02/13/1999

Pubmed ID

9988679

DOI

10.1074/jbc.274.8.4493

Scopus ID

2-s2.0-0033582425   35 Citations

Abstract

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.

Author List

Volkman BF, Anderson ME, Clark KD, Hayakawa Y, Strand MR, Markley JL

Author

Brian F. Volkman PhD Professor in the Biochemistry department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Amino Acid Sequence
Animals
Epidermal Growth Factor
Humans
Intercellular Signaling Peptides and Proteins
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Sequence Data
Moths
Peptides
Protein Structure, Tertiary
Sequence Homology, Amino Acid