 |
PDBsum entry 1hcc
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
J Mol Biol
219:717-725
(1991)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Three-dimensional structure of a complement control protein module in solution.
|
|
D.G.Norman,
P.N.Barlow,
M.Baron,
A.J.Day,
R.B.Sim,
I.D.Campbell.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
The complement control protein (CCP) modules (also known as short consensus
repeats) are defined by a consensus sequence within a stretch of about 60 amino
acid residues. These modules have been identified more than 140 times in over 20
proteins, including 12 proteins of the complement system. The solution structure
of the 16th CCP module from human complement factor H has been determined by a
combination of 2-dimensional nuclear magnetic resonance spectroscopy and
restrained simulated annealing. In all, 548 structurally important nuclear
Overhauser enhancement cross-peaks were quantified as distance restraints and,
together with 41 experimentally measured angle restraints, were incorporated
into a simulated annealing protocol to determine a family of closely related
structures that satisfied the experimental observations. The CCP structure is
shown to be based on a beta-sandwich arrangement; one face made up of three
beta-strands hydrogen-bonded to form a triple-stranded region at its centre and
the other face formed from two separate beta-strands. Both faces of the molecule
contribute highly conserved hydrophobic side-chains to a compact core. The
regions between the beta-strands are composed of both well-defined turns and
less well-defined loops. Analysis of CCP sequence alignments, in light of the
determined structure, reveals a high degree of conservation amongst residues of
obvious structural importance, while almost all insertions, deletions or
replacements observed in the known sequences are found in the less well-defined
loop regions. On the basis of these observations it is postulated that models of
other CCP modules that are based on the structure presented here will be
accurate. Certain families of CCP modules differ from the consensus in that they
contain extra cysteine residues. As a test of structural consensus, the extra
disulphide bridges are shown to be easily accommodated within the determined CCP
model.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
A.Láng,
K.Szilágyi,
B.Major,
P.Gál,
P.Závodszky,
and
A.Perczel
(2010).
Intermodule cooperativity in the structure and dynamics of consecutive complement control modules in human C1r: structural biology.
|
| |
FEBS J,
277,
3986-3998.
|
|
|
|
|
|
|
B.D.Persson,
N.B.Schmitz,
C.Santiago,
G.Zocher,
M.Larvie,
U.Scheu,
J.M.Casasnovas,
and
T.Stehle
(2010).
Structure of the extracellular portion of CD46 provides insights into its interactions with complement proteins and pathogens.
|
| |
PLoS Pathog,
6,
0.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
G.J.Kotwal
(2010).
Influence of glycosylation and oligomerization of vaccinia virus complement control protein on level and pattern of functional activity and immunogenicity.
|
| |
Protein Cell,
1,
1084-1092.
|
|
|
|
|
|
|
C.Parthier,
S.Reedtz-Runge,
R.Rudolph,
and
M.T.Stubbs
(2009).
Passing the baton in class B GPCRs: peptide hormone activation via helix induction?
|
| |
Trends Biochem Sci,
34,
303-310.
|
|
|
|
|
|
|
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.
|
| |
J Biol Chem,
284,
19637-19649.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
M.Okroj,
L.Mark,
A.Stokowska,
S.W.Wong,
N.Rose,
D.J.Blackbourn,
B.O.Villoutreix,
O.B.Spiller,
and
A.M.Blom
(2009).
Characterization of the Complement Inhibitory Function of Rhesus Rhadinovirus Complement Control Protein (RCP).
|
| |
J Biol Chem,
284,
505-514.
|
|
|
|
|
|
|
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.
|
| |
Acta Crystallogr D Biol Crystallogr,
65,
266-274.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
A.P.Herbert,
J.A.Deakin,
C.Q.Schmidt,
B.S.Blaum,
C.Egan,
V.P.Ferreira,
M.K.Pangburn,
M.Lyon,
D.Uhrín,
and
P.N.Barlow
(2007).
Structure shows that a glycosaminoglycan and protein recognition site in factor H is perturbed by age-related macular degeneration-linked single nucleotide polymorphism.
|
| |
J Biol Chem,
282,
18960-18968.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
A.V.Pshezhetsky,
M.Fedjaev,
L.Ashmarina,
A.Mazur,
L.Budman,
D.Sinnett,
D.Labuda,
J.F.Beaulieu,
D.Ménard,
I.Nifant'ev,
and
E.Levy
(2007).
Subcellular proteomics of cell differentiation: quantitative analysis of the plasma membrane proteome of Caco-2 cells.
|
| |
Proteomics,
7,
2201-2215.
|
|
|
|
|
|
|
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.
|
| |
Acta Crystallogr Sect F Struct Biol Cryst Commun,
63,
480-483.
|
|
|
|
|
|
|
C.Parthier,
M.Kleinschmidt,
P.Neumann,
R.Rudolph,
S.Manhart,
D.Schlenzig,
J.Fanghänel,
J.U.Rahfeld,
H.U.Demuth,
and
M.T.Stubbs
(2007).
Crystal structure of the incretin-bound extracellular domain of a G protein-coupled receptor.
|
| |
Proc Natl Acad Sci U S A,
104,
13942-13947.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
L.Mark,
O.B.Spiller,
M.Okroj,
S.Chanas,
J.A.Aitken,
S.W.Wong,
B.Damania,
A.M.Blom,
and
D.J.Blackbourn
(2007).
Molecular characterization of the rhesus rhadinovirus (RRV) ORF4 gene and the RRV complement control protein it encodes.
|
| |
J Virol,
81,
4166-4176.
|
|
|
|
|
|
|
S.K.Olsen,
N.Ota,
S.Kishishita,
M.Kukimoto-Niino,
K.Murayama,
H.Uchiyama,
M.Toyama,
T.Terada,
M.Shirouzu,
O.Kanagawa,
and
S.Yokoyama
(2007).
Crystal Structure of the Interleukin-15{middle dot}Interleukin-15 Receptor {alpha} Complex: INSIGHTS INTO TRANS AND CIS PRESENTATION.
|
| |
J Biol Chem,
282,
37191-37204.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
A.P.Herbert,
D.Uhrín,
M.Lyon,
M.K.Pangburn,
and
P.N.Barlow
(2006).
Disease-associated sequence variations congregate in a polyanion recognition patch on human factor H revealed in three-dimensional structure.
|
| |
J Biol Chem,
281,
16512-16520.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
A.Quéméner,
J.Bernard,
E.Mortier,
A.Plet,
Y.Jacques,
and
V.Tran
(2006).
Docking of human interleukin-15 to its specific receptor alpha chain: correlation between molecular modeling and mutagenesis experimental data.
|
| |
Proteins,
65,
623-636.
|
|
|
|
|
|
|
C.Licht,
S.Heinen,
M.Józsi,
I.Löschmann,
R.E.Saunders,
S.J.Perkins,
R.Waldherr,
C.Skerka,
M.Kirschfink,
B.Hoppe,
and
P.F.Zipfel
(2006).
Deletion of Lys224 in regulatory domain 4 of Factor H reveals a novel pathomechanism for dense deposit disease (MPGN II).
|
| |
Kidney Int,
70,
42-50.
|
|
|
|
|
|
|
E.Mortier,
A.Quéméner,
P.Vusio,
I.Lorenzen,
Y.Boublik,
J.Grötzinger,
A.Plet,
and
Y.Jacques
(2006).
Soluble interleukin-15 receptor alpha (IL-15R alpha)-sushi as a selective and potent agonist of IL-15 action through IL-15R beta/gamma. Hyperagonist IL-15 x IL-15R alpha fusion proteins.
|
| |
J Biol Chem,
281,
1612-1619.
|
|
|
|
|
|
|
I.Lorenzen,
A.J.Dingley,
Y.Jacques,
and
J.Grötzinger
(2006).
The structure of the interleukin-15 alpha receptor and its implications for ligand binding.
|
| |
J Biol Chem,
281,
6642-6647.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
N.Ishikawa,
Y.Daigo,
A.Takano,
M.Taniwaki,
T.Kato,
S.Tanaka,
W.Yasui,
Y.Takeshima,
K.Inai,
H.Nishimura,
E.Tsuchiya,
N.Kohno,
and
Y.Nakamura
(2006).
Characterization of SEZ6L2 cell-surface protein as a novel prognostic marker for lung cancer.
|
| |
Cancer Sci,
97,
737-745.
|
|
|
|
|
|
|
O.B.Spiller,
L.Mark,
C.E.Blue,
D.G.Proctor,
J.A.Aitken,
A.M.Blom,
and
D.J.Blackbourn
(2006).
Dissecting the regions of virion-associated Kaposi's sarcoma-associated herpesvirus complement control protein required for complement regulation and cell binding.
|
| |
J Virol,
80,
4068-4078.
|
|
|
|
|
|
|
S.J.Clark,
V.A.Higman,
B.Mulloy,
S.J.Perkins,
S.M.Lea,
R.B.Sim,
and
A.J.Day
(2006).
His-384 allotypic variant of factor H associated with age-related macular degeneration has different heparin binding properties from the non-disease-associated form.
|
| |
J Biol Chem,
281,
24713-24720.
|
|
|
|
|
|
|
P.M.Callenbach,
E.H.van den Boogerd,
R.F.de Coo,
R.ten Houten,
J.C.Oosterwijk,
G.Hageman,
R.R.Frants,
O.F.Brouwer,
and
A.M.van den Maagdenberg
(2005).
Refinement of the chromosome 16 locus for benign familial infantile convulsions.
|
| |
Clin Genet,
67,
517-525.
|
|
|
|
|
|
|
J.Bernard,
C.Harb,
E.Mortier,
A.Quéméner,
R.H.Meloen,
C.Vermot-Desroches,
J.Wijdeness,
P.van Dijken,
J.Grötzinger,
J.W.Slootstra,
A.Plet,
and
Y.Jacques
(2004).
Identification of an interleukin-15alpha receptor-binding site on human interleukin-15.
|
| |
J Biol Chem,
279,
24313-24322.
|
|
|
|
|
|
|
J.White,
P.Lukacik,
D.Esser,
M.Steward,
N.Giddings,
J.R.Bright,
S.J.Fritchley,
B.P.Morgan,
S.M.Lea,
G.P.Smith,
and
R.A.Smith
(2004).
Biological activity, membrane-targeting modification, and crystallization of soluble human decay accelerating factor expressed in E. coli.
|
| |
Protein Sci,
13,
2406-2415.
|
|
|
|
|
|
|
L.Mark,
W.H.Lee,
O.B.Spiller,
D.Proctor,
D.J.Blackbourn,
B.O.Villoutreix,
and
A.M.Blom
(2004).
The Kaposi's sarcoma-associated herpesvirus complement control protein mimics human molecular mechanisms for inhibition of the complement system.
|
| |
J Biol Chem,
279,
45093-45101.
|
|
|
|
|
|
|
P.Lukacik,
P.Roversi,
J.White,
D.Esser,
G.P.Smith,
J.Billington,
P.A.Williams,
P.M.Rudd,
M.R.Wormald,
D.J.Harvey,
M.D.Crispin,
C.M.Radcliffe,
R.A.Dwek,
D.J.Evans,
B.P.Morgan,
R.A.Smith,
and
S.M.Lea
(2004).
Complement regulation at the molecular level: the structure of decay-accelerating factor.
|
| |
Proc Natl Acad Sci U S A,
101,
1279-1284.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
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.
|
| |
Acta Crystallogr D Biol Crystallogr,
60,
936-938.
|
|
|
|
|
|
|
Y.Nakayama,
N.Nara,
Y.Kawakita,
Y.Takeshima,
M.Arakawa,
M.Katoh,
S.Morita,
K.Iwatsuki,
K.Tanaka,
S.Okamoto,
T.Kitamura,
N.Seki,
R.Matsuda,
M.Matsuo,
K.Saito,
and
T.Hara
(2004).
Cloning of cDNA encoding a regeneration-associated muscle protease whose expression is attenuated in cell lines derived from Duchenne muscular dystrophy patients.
|
| |
Am J Pathol,
164,
1773-1782.
|
|
|
|
|
|
|
J.H.Webb,
B.O.Villoutreix,
B.Dahlbäck,
and
A.M.Blom
(2003).
Role of CCP2 of the C4b-binding protein beta-chain in protein S binding evaluated by mutagenesis and monoclonal antibodies.
|
| |
Eur J Biochem,
270,
93.
|
|
|
|
|
|
|
O.B.Spiller,
D.J.Blackbourn,
L.Mark,
D.G.Proctor,
and
A.M.Blom
(2003).
Functional activity of the complement regulator encoded by Kaposi's sarcoma-associated herpesvirus.
|
| |
J Biol Chem,
278,
9283-9289.
|
|
|
|
|
|
|
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.
|
| |
J Biol Chem,
278,
10691-10696.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
L.S.Laursen,
M.T.Overgaard,
K.Weyer,
H.B.Boldt,
P.Ebbesen,
M.Christiansen,
L.Sottrup-Jensen,
L.C.Giudice,
and
C.Oxvig
(2002).
Cell surface targeting of pregnancy-associated plasma protein A proteolytic activity. Reversible adhesion is mediated by two neighboring short consensus repeats.
|
| |
J Biol Chem,
277,
47225-47234.
|
|
|
|
|
|
|
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.
|
| |
Immunopharmacology,
49,
103-116.
|
|
|
|
|
|
|
G.Lindahl,
U.Sjöbring,
and
E.Johnsson
(2000).
Human complement regulators: a major target for pathogenic microorganisms.
|
| |
Curr Opin Immunol,
12,
44-51.
|
|
|
|
|
|
|
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.
|
| |
J Biol Chem,
274,
19237-19245.
|
|
|
|
|
|
|
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.
|
| |
EMBO J,
18,
5166-5174.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
S.Dubois,
F.Magrangeas,
P.Lehours,
S.Raher,
J.Bernard,
O.Boisteau,
S.Leroy,
S.Minvielle,
A.Godard,
and
Y.Jacques
(1999).
Natural splicing of exon 2 of human interleukin-15 receptor alpha-chain mRNA results in a shortened form with a distinct pattern of expression.
|
| |
J Biol Chem,
274,
26978-26984.
|
|
|
|
|
|
|
S.Lea,
R.Powell,
and
D.Evans
(1999).
Crystallization and preliminary X-ray diffraction analysis of a biologically active fragment of CD55.
|
| |
Acta Crystallogr D Biol Crystallogr,
55,
1198-1200.
|
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
S.M.Scesney,
S.C.Makrides,
M.L.Gosselin,
P.J.Ford,
B.M.Andrews,
E.G.Hayman,
and
H.C.Marsh
(1996).
A soluble deletion mutant of the human complement receptor type 1, which lacks the C4b binding site, is a selective inhibitor of the alternative complement pathway.
|
| |
Eur J Immunol,
26,
1729-1735.
|
|
|
|
|
|
|
D.E.Hourcade,
L.M.Wagner,
and
T.J.Oglesby
(1995).
Analysis of the short consensus repeats of human complement factor B by site-directed mutagenesis.
|
| |
J Biol Chem,
270,
19716-19722.
|
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
P.Bamborough,
C.J.Hedgecock,
and
W.G.Richards
(1994).
The interleukin-2 and interleukin-4 receptors studied by molecular modelling.
|
| |
Structure,
2,
839-851.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
D.T.Fearon
(1993).
The CD19-CR2-TAPA-1 complex, CD45 and signaling by the antigen receptor of B lymphocytes.
|
| |
Curr Opin Immunol,
5,
341-348.
|
|
|
|
|
|
|
R.B.Sim,
K.Kölble,
M.A.McAleer,
O.Dominguez,
and
V.M.Dee
(1993).
Genetics and deficiencies of the soluble regulatory proteins of the complement system.
|
| |
Int Rev Immunol,
10,
65-86.
|
|
|
|
|
|
|
A.Steinkasserer,
P.N.Barlow,
A.C.Willis,
Z.Kertesz,
I.D.Campbell,
R.B.Sim,
and
D.G.Norman
(1992).
Activity, disulphide mapping and structural modelling of the fifth domain of human beta 2-glycoprotein I.
|
| |
FEBS Lett,
313,
193-197.
|
|
|
|
|
|
|
M.Krych,
J.P.Atkinson,
and
V.M.Holers
(1992).
Complement receptors.
|
| |
Curr Opin Immunol,
4,
8.
|
|
|
|
|
|
|
W.J.Chazin
(1992).
NMR structures and methodology.
|
| |
Curr Opin Biotechnol,
3,
326-332.
|
|
|
|
|
|
|
D.R.Martin,
A.Yuryev,
K.R.Kalli,
D.T.Fearon,
and
J.M.Ahearn
(1991).
Determination of the structural basis for selective binding of Epstein-Barr virus to human complement receptor type 2.
|
| |
J Exp Med,
174,
1299-1311.
|
|
|
|
|
|
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.
|
|
Links
