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J Biol Chem, Vol. 274, Issue 8, 4493-4496, February 19, 1999
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From the 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 Å 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 National Magnetic Resonance Facility at
Madison, Department of Biochemistry, University of Wisconsin-Madison,
Madison, Wisconsin 53706-1544, the ¶ Department of Entomology,
University of Wisconsin-Madison, Madison, Wisconsin 53706, and the
Biochemical Laboratory, Institute of Low Temperature Science,
Hokkaido University, Sapporo 060-0819, Japan
-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.
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