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PDBsum entry 2wnv
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Immune system
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PDB id
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2wnv
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Contents |
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132 a.a.
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132 a.a.
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129 a.a.
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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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Complex between c1q globular heads and deoxyribose
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Structure:
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Complement c1q subcomponent subunit a. Chain: a, d. Fragment: c-terminal globular region, residues 112-245. Synonym: c1q chain a. Complement c1q subcomponent subunit b. Chain: b, e. Fragment: c terminal globular domain, residues 116-251. Synonym: c1q chain b. Complement c1q subcomponent subunit c.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Organism_taxid: 9606
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Resolution:
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1.25Å
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R-factor:
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0.176
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R-free:
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0.202
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Authors:
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V.Garlatti,A.Chouquet,T.Lunardi,N.M.Thielens,G.J.Arlaud,C.Gaboriaud
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Key ref:
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V.Garlatti
et al.
(2010).
Cutting edge: C1q binds deoxyribose and heparan sulfate through neighboring sites of its recognition domain.
J Immunol,
185,
808-812.
PubMed id:
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Date:
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20-Jul-09
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Release date:
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26-May-10
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PROCHECK
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Headers
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References
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P02745
(C1QA_HUMAN) -
Complement C1q subcomponent subunit A from Homo sapiens
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Seq:
Struc:
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245 a.a.
132 a.a.
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J Immunol
185:808-812
(2010)
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PubMed id:
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Cutting edge: C1q binds deoxyribose and heparan sulfate through neighboring sites of its recognition domain.
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V.Garlatti,
A.Chouquet,
T.Lunardi,
R.Vivès,
H.Païdassi,
H.Lortat-Jacob,
N.M.Thielens,
G.J.Arlaud,
C.Gaboriaud.
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ABSTRACT
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C1q, the recognition subunit of the C1 complex of complement, is an archetypal
pattern recognition molecule with the striking ability to sense a wide variety
of targets, including a number of altered self-motifs. The recognition
properties of its globular domain were further deciphered by means of x-ray
crystallography using deoxy-D-ribose and heparan sulfate as ligands. Highly
specific recognition of deoxy-D-ribose, involving interactions with Arg C98, Arg
C111, and Asn C113, was observed at 1.2 A resolution. Heparin-derived
tetrasaccharide interacted more loosely through Lys C129, Tyr C155, and Trp
C190. These data together with previous findings define a unique binding area
exhibiting both polyanion and deoxy-D-ribose recognition properties, located on
the inner face of C1q. DNA and heparin compete for C1q binding but are poor C1
activators compared with immune complexes. How the location of this binding area
in C1q may regulate the level of C1 activation is discussed.
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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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H.Païdassi,
P.Tacnet-Delorme,
M.Verneret,
C.Gaboriaud,
G.Houen,
K.Duus,
W.L.Ling,
G.J.Arlaud,
and
P.Frachet
(2011).
Investigations on the C1q-calreticulin-phosphatidylserine interactions yield new insights into apoptotic cell recognition.
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J Mol Biol,
408,
277-290.
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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.
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Links
