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Immune system
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PDB id
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2rkq
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Contents |
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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Cellular component
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extracellular region
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1 term
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Biological process
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innate immune response
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3 terms
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Biochemical function
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protein binding
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3 terms
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DOI no:
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Mol Immunol
45:2521-2530
(2008)
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PubMed id:
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Crystal structure of Drosophila PGRP-SD suggests binding to DAP-type but not lysine-type peptidoglycan.
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P.Leone,
V.Bischoff,
C.Kellenberger,
C.Hetru,
J.Royet,
A.Roussel.
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ABSTRACT
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In Drosophila the synthesis of antimicrobial peptides in response to microbial
infections is under the control of the Toll and immune deficiency (Imd)
signaling pathways. The Toll signaling pathway responds mainly to Gram-positive
bacterial and fungal infection while the Imd pathway mediates the response to
Gram-negative bacteria. Microbial recognition upstream of Toll involves, at
least in part, peptidoglycan recognition proteins (PGRPs). The sensing of
Gram-positive bacteria is mediated by the pattern recognition receptors PGRP-SA
and Gram-negative binding protein 1 (GNBP1) that cooperate to detect the
presence of lysine-type peptidoglycan in the host. Recently it has been shown
that a loss-of-function mutation in peptidoglycan recognition protein SD
(PGRP-SD) severely exacerbates the PGRP-SA and GNBP1 mutant phenotypes. Here we
have solved the crystal structure of PGRP-SD at 1.5A resolution. Comparison with
available structures of PGRPs in complex with their peptidoglycan (PGN) ligand
strongly suggests a diaminopimelic acid (DAP) specificity for PGRP-SD. This
result is supported by pull-down assays with insoluble PGNs. In addition we show
that Toll pathway activation after infection by DAP-type PGN containing bacteria
is clearly reduced in PGRP-SD mutant flies. Our hypothesis is that the role of
PGRP-SD is the recognition of DAP-type PGNs responsible for the activation of
the Toll pathway by Gram-negative bacteria.
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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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N.Basbous,
F.Coste,
P.Leone,
R.Vincentelli,
J.Royet,
C.Kellenberger,
and
A.Roussel
(2011).
The Drosophila peptidoglycan-recognition protein LF interacts with peptidoglycan-recognition protein LC to downregulate the Imd pathway.
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EMBO Rep, 12,
327-333.
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PDB codes:
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S.Meister,
B.Agianian,
F.Turlure,
A.Relógio,
I.Morlais,
F.C.Kafatos,
and
G.K.Christophides
(2009).
Anopheles gambiae PGRPLC-mediated defense against bacteria modulates infections with malaria parasites.
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PLoS Pathog, 5,
e1000542.
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Y.Mishima,
J.Quintin,
V.Aimanianda,
C.Kellenberger,
F.Coste,
C.Clavaud,
C.Hetru,
J.A.Hoffmann,
J.P.Latgé,
D.Ferrandon,
and
A.Roussel
(2009).
The N-terminal domain of Drosophila Gram-negative binding protein 3 (GNBP3) defines a novel family of fungal pattern recognition receptors.
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J Biol Chem, 284,
28687-28697.
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PDB code:
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M.S.Dionne,
and
D.S.Schneider
(2008).
Models of infectious diseases in the fruit fly Drosophila melanogaster.
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Dis Model Mech, 1,
43-49.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
