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PDBsum entry 1hfh
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Contents |
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* Residue conservation analysis
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J Mol Biol
232:268-284
(1993)
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PubMed id:
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Solution structure of a pair of complement modules by nuclear magnetic resonance.
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P.N.Barlow,
A.Steinkasserer,
D.G.Norman,
B.Kieffer,
A.P.Wiles,
R.B.Sim,
I.D.Campbell.
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ABSTRACT
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A portion of human complement factor H spanning the 15th (H15) and 16th (H16) of
its 20 modules, has been expressed in a yeast vector and subjected to structure
determination in solution using two-dimensional 1H-NMR. The structure of H15 is
very similar to that already established for the fifth module of factor H and
H16, consistent with the view that all such complement control (C-) modules
share a common overall topology. In addition, the tertiary structures of the
component modules of the H15-16 pair are very similar to those of the modules
when expressed individually, implying that each folds entirely autonomously
within intact factor H. Aromatic residues in the third turn of H15 and the
second turn of H16, together with a leucine residue from the linker region,
contribute to a small intermodular interface. Comparatively few nuclear
Overhauser effects were observable between protons on different modules.
Consequently, a wide range of angles of "twist" (131 (+/- 146) degrees, mean
value (+/- 1 standard deviation)), i.e. rotation about the long axis of one
module with respect to the other, exists in the family of structures generated
on the basis of the experimental data. However, much smaller variations occur in
the two, orthogonal, angles (175 (+/- 12) degrees and 103 (+/- 6) degrees) that
describe the "tilt". These observations may suggest upper limits on the relative
flexibility of the two modules. Models were built to assess the outcome of
applying such restrictions to all the neighbours within a string of 20
C-modules, and the resulting structures compare well with factor H as visualized
by electron microscopy.
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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.P.Morgan,
C.Q.Schmidt,
M.Guariento,
B.S.Blaum,
D.Gillespie,
A.P.Herbert,
D.Kavanagh,
H.D.Mertens,
D.I.Svergun,
C.M.Johansson,
D.Uhrín,
P.N.Barlow,
and
J.P.Hannan
(2011).
Structural basis for engagement by complement factor H of C3b on a self surface.
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Nat Struct Mol Biol,
18,
463-470.
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PDB code:
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R.Nan,
I.Farabella,
F.F.Schumacher,
A.Miller,
J.Gor,
A.C.Martin,
D.T.Jones,
I.Lengyel,
and
S.J.Perkins
(2011).
Zinc binding to the tyr402 and his402 allotypes of complement factor h: possible implications for age-related macular degeneration.
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J Mol Biol,
408,
714-735.
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C.Q.Schmidt,
A.P.Herbert,
H.D.Mertens,
M.Guariento,
D.C.Soares,
D.Uhrin,
A.J.Rowe,
D.I.Svergun,
and
P.N.Barlow
(2010).
The central portion of factor H (modules 10-15) is compact and contains a structurally deviant CCP module.
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J Mol Biol,
395,
105-122.
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PDB code:
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M.K.Pangburn,
N.Rawal,
C.Cortes,
M.N.Alam,
V.P.Ferreira,
and
M.A.Atkinson
(2009).
Polyanion-induced self-association of complement factor H.
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J Immunol,
182,
1061-1068.
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M.M.Phelan,
C.T.Thai,
D.C.Soares,
R.T.Ogata,
P.N.Barlow,
and
J.Bramham
(2009).
Solution Structure of Factor I-like Modules from Complement C7 Reveals a Pair of Follistatin Domains in Compact Pseudosymmetric Arrangement.
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J Biol Chem,
284,
19637-19649.
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PDB code:
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V.Krishnan,
Y.Xu,
K.Macon,
J.E.Volanakis,
and
S.V.Narayana
(2009).
The structure of C2b, a fragment of complement component C2 produced during C3 convertase formation.
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Acta Crystallogr D Biol Crystallogr,
65,
266-274.
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PDB code:
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H.G.Hocking,
A.P.Herbert,
D.Kavanagh,
D.C.Soares,
V.P.Ferreira,
M.K.Pangburn,
D.Uhrín,
and
P.N.Barlow
(2008).
Structure of the N-terminal region of complement factor H and conformational implications of disease-linked sequence variations.
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J Biol Chem,
283,
9475-9487.
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PDB codes:
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B.E.Prosser,
S.Johnson,
P.Roversi,
A.P.Herbert,
B.S.Blaum,
J.Tyrrell,
T.A.Jowitt,
S.J.Clark,
E.Tarelli,
D.Uhrín,
P.N.Barlow,
R.B.Sim,
A.J.Day,
and
S.M.Lea
(2007).
Structural basis for complement factor H linked age-related macular degeneration.
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J Exp Med,
204,
2277-2283.
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PDB codes:
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B.E.Prosser,
S.Johnson,
P.Roversi,
S.J.Clark,
E.Tarelli,
R.B.Sim,
A.J.Day,
and
S.M.Lea
(2007).
Expression, purification, cocrystallization and preliminary crystallographic analysis of sucrose octasulfate/human complement regulator factor H SCRs 6-8.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
63,
480-483.
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L.Zhang,
and
D.Morikis
(2006).
Immunophysical properties and prediction of activities for vaccinia virus complement control protein and smallpox inhibitor of complement enzymes using molecular dynamics and electrostatics.
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Biophys J,
90,
3106-3119.
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R.E.Saunders,
T.H.Goodship,
P.F.Zipfel,
and
S.J.Perkins
(2006).
An interactive web database of factor H-associated hemolytic uremic syndrome mutations: insights into the structural consequences of disease-associated mutations.
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Hum Mutat,
27,
21-30.
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T.S.Jokiranta,
V.P.Jaakola,
M.J.Lehtinen,
M.Pärepalo,
S.Meri,
and
A.Goldman
(2006).
Structure of complement factor H carboxyl-terminus reveals molecular basis of atypical haemolytic uremic syndrome.
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EMBO J,
25,
1784-1794.
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PDB code:
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J.M.O'Leary,
K.Bromek,
G.M.Black,
S.Uhrinova,
C.Schmitz,
X.Wang,
M.Krych,
J.P.Atkinson,
D.Uhrin,
and
P.N.Barlow
(2004).
Backbone dynamics of complement control protein (CCP) modules reveals mobility in binding surfaces.
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Protein Sci,
13,
1238-1250.
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PDB code:
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R.J.Abbott,
V.Knott,
P.Roversi,
S.Neudeck,
P.Lukacik,
P.A.Handford,
and
S.M.Lea
(2004).
Crystallization and preliminary X-ray diffraction analysis of three EGF domains of EMR2, a 7TM immune-system molecule.
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Acta Crystallogr D Biol Crystallogr,
60,
936-938.
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P.Williams,
Y.Chaudhry,
I.G.Goodfellow,
J.Billington,
R.Powell,
O.B.Spiller,
D.J.Evans,
and
S.Lea
(2003).
Mapping CD55 function. The structure of two pathogen-binding domains at 1.7 A.
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J Biol Chem,
278,
10691-10696.
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PDB codes:
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S.Uhrinova,
F.Lin,
G.Ball,
K.Bromek,
D.Uhrin,
M.E.Medof,
and
P.N.Barlow
(2003).
Solution structure of a functionally active fragment of decay-accelerating factor.
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Proc Natl Acad Sci U S A,
100,
4718-4723.
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PDB code:
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A.D.Stuart,
T.A.McKee,
P.A.Williams,
C.Harley,
S.Shen,
D.I.Stuart,
T.D.Brown,
and
S.M.Lea
(2002).
Determination of the structure of a decay accelerating factor-binding clinical isolate of echovirus 11 allows mapping of mutants with altered receptor requirements for infection.
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J Virol,
76,
7694-7704.
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PDB code:
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A.E.Prota,
D.R.Sage,
T.Stehle,
and
J.D.Fingeroth
(2002).
The crystal structure of human CD21: Implications for Epstein-Barr virus and C3d binding.
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Proc Natl Acad Sci U S A,
99,
10641-10646.
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PDB code:
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B.O.Smith,
R.L.Mallin,
M.Krych-Goldberg,
X.Wang,
R.E.Hauhart,
K.Bromek,
D.Uhrin,
J.P.Atkinson,
and
P.N.Barlow
(2002).
Structure of the C3b binding site of CR1 (CD35), the immune adherence receptor.
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Cell,
108,
769-780.
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PDB codes:
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R.J.Hasan,
E.Pawelczyk,
P.T.Urvil,
M.S.Venkatarajan,
P.Goluszko,
J.Kur,
R.Selvarangan,
S.Nowicki,
W.A.Braun,
and
B.J.Nowicki
(2002).
Structure-function analysis of decay-accelerating factor: identification of residues important for binding of the Escherichia coli Dr adhesin and complement regulation.
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Infect Immun,
70,
4485-4493.
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G.Szakonyi,
J.M.Guthridge,
D.Li,
K.Young,
V.M.Holers,
and
X.S.Chen
(2001).
Structure of complement receptor 2 in complex with its C3d ligand.
|
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Science,
292,
1725-1728.
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PDB code:
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J.M.Guthridge,
J.K.Rakstang,
K.A.Young,
J.Hinshelwood,
M.Aslam,
A.Robertson,
M.G.Gipson,
M.R.Sarrias,
W.T.Moore,
M.Meagher,
D.Karp,
J.D.Lambris,
S.J.Perkins,
and
V.M.Holers
(2001).
Structural studies in solution of the recombinant N-terminal pair of short consensus/complement repeat domains of complement receptor type 2 (CR2/CD21) and interactions with its ligand C3dg.
|
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Biochemistry,
40,
5931-5941.
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K.H.Murthy,
S.A.Smith,
V.K.Ganesh,
K.W.Judge,
N.Mullin,
P.N.Barlow,
C.M.Ogata,
and
G.J.Kotwal
(2001).
Crystal structure of a complement control protein that regulates both pathways of complement activation and binds heparan sulfate proteoglycans.
|
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Cell,
104,
301-311.
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PDB codes:
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C.Gaboriaud,
V.Rossi,
I.Bally,
G.J.Arlaud,
and
J.C.Fontecilla-Camps
(2000).
Crystal structure of the catalytic domain of human complement c1s: a serine protease with a handle.
|
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EMBO J,
19,
1755-1765.
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PDB code:
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D.Hourcade,
M.K.Liszewski,
M.Krych-Goldberg,
and
J.P.Atkinson
(2000).
Functional domains, structural variations and pathogen interactions of MCP, DAF and CR1.
|
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Immunopharmacology,
49,
103-116.
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I.Callebaut,
D.Gilgès,
I.Vigon,
and
J.P.Mornon
(2000).
HYR, an extracellular module involved in cellular adhesion and related to the immunoglobulin-like fold.
|
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Protein Sci,
9,
1382-1390.
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L.Spendlove,
L.Li,
V.Potter,
D.Christiansen,
B.E.Loveland,
and
L.G.Durrant
(2000).
A therapeutic human anti-idiotypic antibody mimics CD55 in three distinct regions.
|
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Eur J Immunol,
30,
2944-2953.
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A.E.Oran,
and
D.E.Isenman
(1999).
Identification of residues within the 727-767 segment of human complement component C3 important for its interaction with factor H and with complement receptor 1 (CR1, CD35).
|
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J Biol Chem,
274,
5120-5130.
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A.M.Blom,
J.Webb,
B.O.Villoutreix,
and
B.Dahlbäck
(1999).
A cluster of positively charged amino acids in the C4BP alpha-chain is crucial for C4b binding and factor I cofactor function.
|
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J Biol Chem,
274,
19237-19245.
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B.Bouma,
P.G.de Groot,
J.M.van den Elsen,
R.B.Ravelli,
A.Schouten,
M.J.Simmelink,
R.H.Derksen,
J.Kroon,
and
P.Gros
(1999).
Adhesion mechanism of human beta(2)-glycoprotein I to phospholipids based on its crystal structure.
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EMBO J,
18,
5166-5174.
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PDB code:
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B.Z.Schmidt,
N.L.Fowler,
T.Hidvegi,
D.H.Perlmutter,
and
H.R.Colten
(1999).
Disruption of disulfide bonds is responsible for impaired secretion in human complement factor H deficiency.
|
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J Biol Chem,
274,
11782-11788.
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D.Mossakowska,
I.Dodd,
W.Pindar,
and
R.A.Smith
(1999).
Structure-activity relationships within the N-terminal short consensus repeats (SCR) of human CR1 (C3b/C4b receptor, CD35): SCR 3 plays a critical role in inhibition of the classical and alternative pathways of complement activation.
|
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Eur J Immunol,
29,
1955-1965.
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E.C.Hsu,
S.Sabatinos,
F.J.Hoedemaeker,
D.R.Rose,
and
C.D.Richardson
(1999).
Use of site-specific mutagenesis and monoclonal antibodies to map regions of CD46 that interact with measles virus H protein.
|
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Virology,
258,
314-326.
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H.Okkels,
T.E.Rasmussen,
D.K.Sanghera,
M.I.Kamboh,
and
T.Kristensen
(1999).
Structure of the human beta2-glycoprotein I (apolipoprotein H) gene.
|
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Eur J Biochem,
259,
435-440.
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J.M.Casasnovas,
M.Larvie,
and
T.Stehle
(1999).
Crystal structure of two CD46 domains reveals an extended measles virus-binding surface.
|
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EMBO J,
18,
2911-2922.
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PDB code:
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M.D.Kirkitadze,
M.Krych,
D.Uhrin,
D.T.Dryden,
B.O.Smith,
A.Cooper,
X.Wang,
R.Hauhart,
J.P.Atkinson,
and
P.N.Barlow
(1999).
Independently melting modules and highly structured intermodular junctions within complement receptor type 1.
|
| |
Biochemistry,
38,
7019-7031.
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R.Schwarzenbacher,
K.Zeth,
K.Diederichs,
A.Gries,
G.M.Kostner,
P.Laggner,
and
R.Prassl
(1999).
Crystal structure of human beta2-glycoprotein I: implications for phospholipid binding and the antiphospholipid syndrome.
|
| |
EMBO J,
18,
6228-6239.
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PDB code:
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S.X.Wang,
G.Cai,
and
S.Sui
(1999).
Intrinsic fluorescence study of the interaction of human apolipoprotein H with phospholipid vesicles.
|
| |
Biochemistry,
38,
9477-9484.
|
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|
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V.Estienne,
C.Blanchet,
P.Niccoli-Sire,
C.Duthoit,
J.M.Durand-Gorde,
C.Geourjon,
D.Baty,
P.Carayon,
and
J.Ruf
(1999).
Molecular model, calcium sensitivity, and disease specificity of a conformational thyroperoxidase B-cell epitope.
|
| |
J Biol Chem,
274,
35313-35317.
|
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|
|
|
|
|
W.M.Prodinger
(1999).
Complement receptor type two (CR2,CR21): a target for influencing the humoral immune response and antigen-trapping.
|
| |
Immunol Res,
20,
187-194.
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B.Nagar,
R.G.Jones,
R.J.Diefenbach,
D.E.Isenman,
and
J.M.Rini
(1998).
X-ray crystal structure of C3d: a C3 fragment and ligand for complement receptor 2.
|
| |
Science,
280,
1277-1281.
|
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PDB code:
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B.O.Villoutreix,
Y.Härdig,
A.Wallqvist,
D.G.Covell,
P.García de Frutos,
and
B.Dahlbäck
(1998).
Structural investigation of C4b-binding protein by molecular modeling: localization of putative binding sites.
|
| |
Proteins,
31,
391-405.
|
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I.D.Campbell
(1998).
The modular architecture of leukocyte cell-surface receptors.
|
| |
Immunol Rev,
163,
11-18.
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M.Krych,
R.Hauhart,
and
J.P.Atkinson
(1998).
Structure-function analysis of the active sites of complement receptor type 1.
|
| |
J Biol Chem,
273,
8623-8629.
|
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A.K.Sharma,
and
M.K.Pangburn
(1997).
Localization by site-directed mutagenesis of the site in human complement factor H that binds to Streptococcus pyogenes M protein.
|
| |
Infect Immun,
65,
484-487.
|
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B.H.Ault,
B.Z.Schmidt,
N.L.Fowler,
C.E.Kashtan,
A.E.Ahmed,
B.A.Vogt,
and
H.R.Colten
(1997).
Human factor H deficiency. Mutations in framework cysteine residues and block in H protein secretion and intracellular catabolism.
|
| |
J Biol Chem,
272,
25168-25175.
|
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C.Mumenthaler,
U.Schneider,
C.J.Buchholz,
D.Koller,
W.Braun,
and
R.Cattaneo
(1997).
A 3D model for the measles virus receptor CD46 based on homology modeling, Monte Carlo simulations, and hemagglutinin binding studies.
|
| |
Protein Sci,
6,
588-597.
|
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E.C.Hsu,
R.E.Dörig,
F.Sarangi,
A.Marcil,
C.Iorio,
and
C.D.Richardson
(1997).
Artificial mutations and natural variations in the CD46 molecules from human and monkey cells define regions important for measles virus binding.
|
| |
J Virol,
71,
6144-6154.
|
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M.Lacroix,
V.Rossi,
C.Gaboriaud,
S.Chevallier,
M.Jaquinod,
N.M.Thielens,
J.Gagnon,
and
G.J.Arlaud
(1997).
Structure and assembly of the catalytic region of human complement protease C1r: a three-dimensional model based on chemical cross-linking and homology modeling.
|
| |
Biochemistry,
36,
6270-6282.
|
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|
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X.He,
L.Shen,
A.C.Malmborg,
K.J.Smith,
B.Dahlback,
and
S.Linse
(1997).
Binding site for C4b-binding protein in vitamin K-dependent protein S fully contained in carboxy-terminal laminin-G-type repeats. A study using recombinant factor IX-protein S chimeras and surface plasmon resonance.
|
| |
Biochemistry,
36,
3745-3754.
|
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|
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A.K.Sharma,
and
M.K.Pangburn
(1996).
Identification of three physically and functionally distinct binding sites for C3b in human complement factor H by deletion mutagenesis.
|
| |
Proc Natl Acad Sci U S A,
93,
10996-11001.
|
|
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|
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C.J.Buchholz,
U.Schneider,
P.Devaux,
D.Gerlier,
and
R.Cattaneo
(1996).
Cell entry by measles virus: long hybrid receptors uncouple binding from membrane fusion.
|
| |
J Virol,
70,
3716-3723.
|
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|
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|
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M.Sunnerhagen,
G.A.Olah,
J.Stenflo,
S.Forsén,
T.Drakenberg,
and
J.Trewhella
(1996).
The relative orientation of Gla and EGF domains in coagulation factor X is altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering study.
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| |
Biochemistry,
35,
11547-11559.
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PDB codes:
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P.Bork,
A.K.Downing,
B.Kieffer,
and
I.D.Campbell
(1996).
Structure and distribution of modules in extracellular proteins.
|
| |
Q Rev Biophys,
29,
119-167.
|
|
|
|
|
|
|
P.García de Frutos,
Y.Härdig,
and
B.Dahlbäck
(1995).
Serum amyloid P component binding to C4b-binding protein.
|
| |
J Biol Chem,
270,
26950-26955.
|
|
|
|
|
|
|
D.L.Bodian,
E.Y.Jones,
K.Harlos,
D.I.Stuart,
and
S.J.Davis
(1994).
Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution.
|
| |
Structure,
2,
755-766.
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PDB code:
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D.R.Martin,
R.L.Marlowe,
and
J.M.Ahearn
(1994).
Determination of the role for CD21 during Epstein-Barr virus infection of B-lymphoblastoid cells.
|
| |
J Virol,
68,
4716-4726.
|
|
|
|
|
|
|
G.Wagner,
and
D.F.Wyss
(1994).
Cell surface adhesion receptors.
|
| |
Curr Opin Struct Biol,
4,
841-851.
|
|
|
|
|
|
|
I.D.Campbell,
and
A.K.Downing
(1994).
Building protein structure and function from modular units.
|
| |
Trends Biotechnol,
12,
168-172.
|
|
|
|
|
|
|
I.D.Campbell,
and
C.Spitzfaden
(1994).
Building proteins with fibronectin type III modules.
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| |
Structure,
2,
333-337.
|
|
|
|
|
|
|
P.Bamborough,
C.J.Hedgecock,
and
W.G.Richards
(1994).
The interleukin-2 and interleukin-4 receptors studied by molecular modelling.
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| |
Structure,
2,
839-851.
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PDB codes:
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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
code is
shown on the right.
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Links
