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PDBsum entry 1c5a
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Complement factor
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PDB id
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1c5a
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Contents |
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* Residue conservation analysis
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DOI no:
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Biochemistry
29:2895-2905
(1990)
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PubMed id:
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Three-dimensional structure of porcine C5adesArg from 1H nuclear magnetic resonance data.
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M.P.Williamson,
V.S.Madison.
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ABSTRACT
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Two-dimensional nuclear magnetic resonance spectra of porcine C5adesArg (73
residues) have been used to construct a list of 34 hydrogen bonds, 27 dihedral
angle constraints, and 151 distance constraints, derived from nuclear Overhauser
effect data. These constraints were used in restrained molecular dynamics
calculations on residues 1-65 of C5a, starting from a folded structure modeled
on the crystal structure of a homologous protein, C3a. Forty-one structures have
been calculated, which fall into three similar families with few violations of
the imposed constraints. Structures in the most populated family have a
root-mean-square deviation from the average structure of 1.02 A for the C alpha
atoms, with good definition of the internal residues. There is good agreement
between the calculated structures and other nuclear magnetic resonance data. The
structure is very similar to that recently reported for human C5a [Zuiderweg et
al. (1989) Biochemistry 28, 172-185]. Some biological implications of these
structures are 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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W.J.Cook,
N.Galakatos,
W.C.Boyar,
R.L.Walter,
and
S.E.Ealick
(2010).
Structure of human desArg-C5a.
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Acta Crystallogr D Biol Crystallogr,
66,
190-197.
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PDB codes:
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Y.Wang,
Y.Zhang,
W.Han,
D.Li,
L.Tian,
C.Yin,
and
D.Ma
(2008).
Two C-terminal peptides of human CKLF1 interact with the chemokine receptor CCR4.
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Int J Biochem Cell Biol,
40,
909-919.
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M.Pasupuleti,
B.Walse,
E.A.Nordahl,
M.Mörgelin,
M.Malmsten,
and
A.Schmidtchen
(2007).
Preservation of antimicrobial properties of complement peptide C3a, from invertebrates to humans.
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J Biol Chem,
282,
2520-2528.
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I.S.Hagemann,
K.D.Narzinski,
D.H.Floyd,
and
T.J.Baranski
(2006).
Random mutagenesis of the complement factor 5a (C5a) receptor N terminus provides a structural constraint for C5a docking.
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J Biol Chem,
281,
36783-36792.
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C.K.Brown,
Z.Y.Gu,
Y.V.Matsuka,
S.S.Purushothaman,
L.A.Winter,
P.P.Cleary,
S.B.Olmsted,
D.H.Ohlendorf,
and
C.A.Earhart
(2005).
Structure of the streptococcal cell wall C5a peptidase.
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Proc Natl Acad Sci U S A,
102,
18391-18396.
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PDB code:
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V.Wittamer,
F.Grégoire,
P.Robberecht,
G.Vassart,
D.Communi,
and
M.Parmentier
(2004).
The C-terminal nonapeptide of mature chemerin activates the chemerin receptor with low nanomolar potency.
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J Biol Chem,
279,
9956-9962.
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D.A.Debe,
M.J.Carlson,
and
W.A.Goddard
(1999).
The topomer-sampling model of protein folding.
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Proc Natl Acad Sci U S A,
96,
2596-2601.
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Z.Chen,
X.Zhang,
N.C.Gonnella,
T.C.Pellas,
W.C.Boyar,
and
F.Ni
(1998).
Residues 21-30 within the extracellular N-terminal region of the C5a receptor represent a binding domain for the C5a anaphylatoxin.
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J Biol Chem,
273,
10411-10419.
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X.Zhang,
W.Boyar,
M.J.Toth,
L.Wennogle,
and
N.C.Gonnella
(1997).
Structural definition of the C5a C terminus by two-dimensional nuclear magnetic resonance spectroscopy.
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Proteins,
28,
261-267.
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PDB code:
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X.Zhang,
W.Boyar,
N.Galakatos,
and
N.C.Gonnella
(1997).
Solution structure of a unique C5a semi-synthetic antagonist: implications in receptor binding.
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Protein Sci,
6,
65-72.
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PDB code:
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P.Bork,
A.K.Downing,
B.Kieffer,
and
I.D.Campbell
(1996).
Structure and distribution of modules in extracellular proteins.
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Q Rev Biophys,
29,
119-167.
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L.Cui,
D.F.Carney,
and
T.E.Hugli
(1994).
Primary structure and functional characterization of rat C5a: an anaphylatoxin with unusually high potency.
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Protein Sci,
3,
1169-1177.
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P.Bubeck,
J.Grötzinger,
M.Winkler,
J.Köhl,
A.Wollmer,
A.Klos,
and
W.Bautsch
(1994).
Site-specific mutagenesis of residues in the human C5a anaphylatoxin which are involved in possible interaction with the C5a receptor.
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Eur J Biochem,
219,
897-904.
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D.F.Carney,
and
T.E.Hugli
(1993).
Site-specific mutations in the N-terminal region of human C5a that affect interactions of C5a with the neutrophil C5a receptor.
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Protein Sci,
2,
1391-1399.
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M.J.Sutcliffe
(1993).
Representing an ensemble of NMR-derived protein structures by a single structure.
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Protein Sci,
2,
936-944.
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M.W.MacArthur,
and
J.M.Thornton
(1993).
Conformational analysis of protein structures derived from NMR data.
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Proteins,
17,
232-251.
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N.A.van Nuland,
J.Grötzinger,
K.Dijkstra,
R.M.Scheek,
and
G.T.Robillard
(1992).
Determination of the three-dimensional solution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli using multidimensional NMR spectroscopy.
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Eur J Biochem,
210,
881-891.
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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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