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Immune system
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PDB id
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2aph
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Contents |
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* Residue conservation analysis
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PDB id:
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Immune system
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Title:
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Crystal structure of human pgrp-ialphac in complex with mura pentapeptide
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Structure:
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Peptidoglycan recognition protein i-alpha. Chain: a, b. Synonym: peptidoglycan recognition protein intermediate alp i-alpha, pglyrpialpha, peptidoglycan recognition protein 3. Engineered: yes. Muramyl pentapeptide. Chain: c, d. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: pglyrp3, pgrpia. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Other_details: muramyl pentapeptide was synthesized chemica
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Biol. unit:
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Dimer (from
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Resolution:
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2.10Å
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R-factor:
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0.227
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R-free:
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0.267
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Authors:
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R.Guan,A.Roychowdjury,G.Boons,R.A.Mariuzza
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Key ref:
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R.Guan
et al.
(2006).
Crystal structure of human peptidoglycan recognition protein I alpha bound to a muramyl pentapeptide from Gram-positive bacteria.
Protein Sci,
15,
1199-1206.
PubMed id:
DOI:
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Date:
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16-Aug-05
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Release date:
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27-Jun-06
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PROCHECK
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Headers
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References
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Q96LB9
(PGRP3_HUMAN) -
Peptidoglycan recognition protein 3
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Seq:
Struc:
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341 a.a.
165 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Gene Ontology (GO) functional annotation
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Biological process
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peptidoglycan catabolic process
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1 term
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Biochemical function
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N-acetylmuramoyl-L-alanine amidase activity
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2 terms
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DOI no:
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Protein Sci
15:1199-1206
(2006)
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PubMed id:
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Crystal structure of human peptidoglycan recognition protein I alpha bound to a muramyl pentapeptide from Gram-positive bacteria.
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R.Guan,
P.H.Brown,
C.P.Swaminathan,
A.Roychowdhury,
G.J.Boons,
R.A.Mariuzza.
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ABSTRACT
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Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors of
the innate immune system that bind bacterial peptidoglycans (PGNs). We
determined the crystal structure, to 2.1 A resolution, of the C-terminal
PGN-binding domain of human PGRP-I alpha in complex with a muramyl pentapeptide
(MPP) from Gram-positive bacteria containing a complete peptide stem
(L-Ala-D-isoGln-L-Lys-D-Ala-D-Ala). The structure reveals important features not
observed previously in the complex between PGRP-I alpha and a muramyl tripeptide
lacking D-Ala at stem positions 4 and 5. Most notable are ligand-induced
structural rearrangements in the PGN-binding site that are essential for entry
of the C-terminal portion of the peptide stem and for locking MPP in the binding
groove. We propose that similar structural rearrangements to accommodate the PGN
stem likely characterize many PGRPs, both mammalian and insect.
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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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Y.Li,
C.L.Efferson,
R.Ramesh,
G.E.Peoples,
P.Hwu,
and
C.G.Ioannides
(2011).
A peptidoglycan monomer with the glutamine to serine change and basic peptides bind in silico to TLR-2 (403-455).
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Cancer Immunol Immunother, 60,
515-524.
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P.C.Oyston,
M.A.Fox,
S.J.Richards,
and
G.C.Clark
(2009).
Novel peptide therapeutics for treatment of infections.
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J Med Microbiol, 58,
977-987.
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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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J.Royet,
and
R.Dziarski
(2007).
Peptidoglycan recognition proteins: pleiotropic sensors and effectors of antimicrobial defences.
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Nat Rev Microbiol, 5,
264-277.
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R.Guan,
and
R.A.Mariuzza
(2007).
Peptidoglycan recognition proteins of the innate immune system.
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Trends Microbiol, 15,
127-134.
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S.Cho,
Q.Wang,
C.P.Swaminathan,
D.Hesek,
M.Lee,
G.J.Boons,
S.Mobashery,
and
R.A.Mariuzza
(2007).
Structural insights into the bactericidal mechanism of human peptidoglycan recognition proteins.
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Proc Natl Acad Sci U S A, 104,
8761-8766.
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PDB codes:
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L.Wang,
A.N.Weber,
M.L.Atilano,
S.R.Filipe,
N.J.Gay,
and
P.Ligoxygakis
(2006).
Sensing of Gram-positive bacteria in Drosophila: GNBP1 is needed to process and present peptidoglycan to PGRP-SA.
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EMBO J, 25,
5005-5014.
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R.Dziarski,
and
D.Gupta
(2006).
The peptidoglycan recognition proteins (PGRPs).
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Genome Biol, 7,
232.
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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
