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PDBsum entry 1b1v
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DOI no:
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J Biol Chem
274:4493-4496
(1999)
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PubMed id:
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Structure of the insect cytokine peptide plasmatocyte-spreading peptide 1 from Pseudoplusia includens.
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B.F.Volkman,
M.E.Anderson,
K.D.Clark,
Y.Hayakawa,
M.R.Strand,
J.L.Markley.
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ABSTRACT
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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.
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Selected figure(s)
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Figure 1.
Fig. 1. Comparison of the sequences of PSP1 from P.
includens, GBP from P. separata, paralytic peptide from M. sexta
(PP1), and the C-terminal subdomains of human epidermal growth
factor (hEGF) and the hTM5. Highlighted in boldface type are the
cysteine, glycine, and tyrosine residues conserved in the
EGF-like domain family and the corresponding residues of the
insect peptides.
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Figure 6.
Fig. 6. Ribbon diagram of the minimized average structure
of PSP1 with all nonhydrogen side chain atoms shown. The charged
side chains of the -hairpin are
labeled.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(1999,
274,
4493-4496)
copyright 1999.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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K.Anamika,
A.Bhattacharya,
and
N.Srinivasan
(2008).
Analysis of the protein kinome of Entamoeba histolytica.
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Proteins,
71,
995.
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M.R.Kanost,
H.Jiang,
and
X.Q.Yu
(2004).
Innate immune responses of a lepidopteran insect, Manduca sexta.
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Immunol Rev,
198,
97.
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Y.Nakahara,
Y.Kanamori,
M.Kiuchi,
and
M.Kamimura
(2003).
Effects of silkworm paralytic peptide on in vitro hematopoiesis and plasmatocyte spreading.
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Arch Insect Biochem Physiol,
52,
163-174.
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J.Song,
P.Xu,
A.Koutychenko,
and
F.Ni
(2002).
Stability of protein-bound conformations of bioactive peptides: the folded conformation of an epidermal growth factor-like thrombomodulin fragment is similar to that recognized by thrombin.
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Biopolymers,
65,
373-386.
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O.Schmidt,
U.Theopold,
and
M.Strand
(2001).
Innate immunity and its evasion and suppression by hymenopteran endoparasitoids.
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Bioessays,
23,
344-351.
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M.R.Strand,
and
K.D.Clark
(1999).
Plasmatocyte spreading peptide induces spreading of plasmatocytes but represses spreading of granulocytes.
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Arch Insect Biochem Physiol,
42,
213-223.
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X.Q.Yu,
O.Prakash,
and
M.R.Kanost
(1999).
Structure of a paralytic peptide from an insect, Manduca sexta.
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J Pept Res,
54,
256-261.
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PDB code:
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Where a reference describes a PDB structure, the PDB
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