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* Residue conservation analysis
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PDB id:
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Viral protein/immune system
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Title:
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Human adenovirus type 11 knob in complex with domains scr1 and scr2 of cd46 (membrane cofactor protein, mcp)
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Structure:
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Fiber protein. Chain: a, b. Fragment: residues 129-325. Synonym: piv. Engineered: yes. Membrane cofactor protein. Chain: c, d. Fragment: scr1 and scr 2 domains. Synonym: trophoblast leukocyte common antigen, tlx, cd46 antigen.
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Source:
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Human adenovirus 11p. Organism_taxid: 343462. Strain: slobiski. Gene: piv. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens. Human. Organism_taxid: 9606.
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Resolution:
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2.85Å
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R-factor:
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0.238
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R-free:
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0.273
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Authors:
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D.B.Persson,D.M.Reiter,N.Arnberg,T.Stehle
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Key ref:
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B.D.Persson
et al.
(2007).
Adenovirus type 11 binding alters the conformation of its receptor CD46.
Nat Struct Mol Biol,
14,
164-166.
PubMed id:
DOI:
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Date:
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01-Dec-06
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Release date:
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09-Jan-07
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PROCHECK
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Headers
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References
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DOI no:
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Nat Struct Mol Biol
14:164-166
(2007)
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PubMed id:
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Adenovirus type 11 binding alters the conformation of its receptor CD46.
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B.D.Persson,
D.M.Reiter,
M.Marttila,
Y.F.Mei,
J.M.Casasnovas,
N.Arnberg,
T.Stehle.
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ABSTRACT
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Adenoviruses (Ads) are important human pathogens and valuable gene delivery
vehicles. We report here the crystal structure of the species B Ad11 knob
complexed with the Ad11-binding region of its receptor CD46. The conformation of
bound CD46 differs profoundly from its unbound state, with the bent surface
structure straightened into an elongated rod. This mechanism of interaction is
likely to be conserved among many pathogens that target CD46 or related
molecules.
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Selected figure(s)
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Figure 1.
Figure 1. Structure of the Ad11 knob complexed with CD46
SCR1-SCR2. (a) Ribbon drawing of the complex. The three
subunits forming the Ad11 knob are blue, green and gray; bound
CD46 SCR1-SCR2 is red. Glycosylated residues Asn49 and Asn80 are
red. The glycan attached to Asn80 is yellow. (b) Surface
representation of a CD46 SCR1-SCR2 molecule bound to two Ad11
knob protomers, colored as in a. CD46 has been moved away from
the two Ad11 knob protomers by about 5 Å to highlight
shape complementarity. Views in a and b are from opposite
directions. (c) 2F[o] – F[c] electron density map, contoured
at 1.0 and
showing interactions between CD46 and the Ad11 knob.
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Figure 2.
Figure 2. Interaction between the Ad11 knob and CD46 SCR1-SCR2.
(a) Ribbon tracing of the complex, colored as in Figure 1.
(b–d) The three major contact regions (A–C) of Ad11 knob.
Nitrogen and oxygen atoms are blue and red, respectively.
Hydrogen bonds and salt bridges are represented with dashed
lines. (e) Superimposition of SCR2 domains of unliganded^13
(blue) and liganded CD46 (red). The two Ad11 knob protomers
interacting with CD46 are shown in gray. Arrow indicates the
rearrangement of SCR1 upon binding to Ad11 knob. (f) Close-up
view of the interaction. Key residues of CD46 that interact with
Ad11 knob are shown in orange. (g) Structure of unliganded CD46.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Mol Biol
(2007,
14,
164-166)
copyright 2007.
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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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D.Henaff,
S.Salinas,
and
E.J.Kremer
(2011).
An adenovirus traffic update: from receptor engagement to the nuclear pore.
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Future Microbiol,
6,
179-192.
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E.C.Nilsson,
R.J.Storm,
J.Bauer,
S.M.Johansson,
A.Lookene,
J.Ångström,
M.Hedenström,
T.L.Eriksson,
L.Frängsmyr,
S.Rinaldi,
H.J.Willison,
F.Pedrosa Domellöf,
T.Stehle,
and
N.Arnberg
(2011).
The GD1a glycan is a cellular receptor for adenoviruses causing epidemic keratoconjunctivitis.
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Nat Med,
17,
105-109.
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PDB code:
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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.
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PLoS Pathog,
6,
0.
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PDB code:
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C.Santiago,
A.Gutiérrez-Rodríguez,
P.A.Tucker,
T.Stehle,
and
J.M.Casasnovas
(2010).
Crystallization and preliminary crystallographic analysis of the measles virus hemagglutinin in complex with the CD46 receptor.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
66,
91-94.
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C.Santiago,
M.L.Celma,
T.Stehle,
and
J.M.Casasnovas
(2010).
Structure of the measles virus hemagglutinin bound to the CD46 receptor.
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Nat Struct Mol Biol,
17,
124-129.
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PDB code:
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J.G.Smith,
C.M.Wiethoff,
P.L.Stewart,
and
G.R.Nemerow
(2010).
Adenovirus.
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Curr Top Microbiol Immunol,
343,
195-224.
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J.S.Senac,
K.Doronin,
S.J.Russell,
D.F.Jelinek,
P.R.Greipp,
and
M.A.Barry
(2010).
Infection and killing of multiple myeloma by adenoviruses.
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Hum Gene Ther,
21,
179-190.
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K.Cupelli,
S.Müller,
B.D.Persson,
M.Jost,
N.Arnberg,
and
T.Stehle
(2010).
Structure of adenovirus type 21 knob in complex with CD46 reveals key differences in receptor contacts among species B adenoviruses.
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J Virol,
84,
3189-3200.
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PDB codes:
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A.Sharma,
X.Li,
D.S.Bangari,
and
S.K.Mittal
(2009).
Adenovirus receptors and their implications in gene delivery.
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Virus Res,
143,
184-194.
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B.D.Persson,
S.Müller,
D.M.Reiter,
B.B.Schmitt,
M.Marttila,
C.V.Sumowski,
S.Schweizer,
U.Scheu,
C.Ochsenfeld,
N.Arnberg,
and
T.Stehle
(2009).
An arginine switch in the species B adenovirus knob determines high-affinity engagement of cellular receptor CD46.
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J Virol,
83,
673-686.
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PDB codes:
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G.R.Nemerow,
L.Pache,
V.Reddy,
and
P.L.Stewart
(2009).
Insights into adenovirus host cell interactions from structural studies.
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Virology,
384,
380-388.
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H.Matsui,
F.Sakurai,
S.Kurachi,
K.Tashiro,
K.Sugio,
K.Kawabata,
K.Yamanishi,
and
H.Mizuguchi
(2009).
Development of fiber-substituted adenovirus vectors containing foreign peptides in the adenovirus serotype 35 fiber knob.
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Gene Ther,
16,
1050-1057.
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H.Wang,
S.Tuve,
D.D.Erdman,
and
A.Lieber
(2009).
Receptor usage of a newly emergent adenovirus type 14.
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Virology,
387,
436-441.
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L.Sandberg,
P.Papareddy,
J.Silver,
A.Bergh,
and
Y.F.Mei
(2009).
Replication-competent Ad11p vector (RCAd11p) efficiently transduces and replicates in hormone-refractory metastatic prostate cancer cells.
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Hum Gene Ther,
20,
361-373.
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T.Stehle,
and
J.M.Casasnovas
(2009).
Specificity switching in virus-receptor complexes.
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Curr Opin Struct Biol,
19,
181-188.
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|
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|
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W.C.Russell
(2009).
Adenoviruses: update on structure and function.
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J Gen Virol,
90,
1.
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B.Amstutz,
M.Gastaldelli,
S.Kälin,
N.Imelli,
K.Boucke,
E.Wandeler,
J.Mercer,
S.Hemmi,
and
U.F.Greber
(2008).
Subversion of CtBP1-controlled macropinocytosis by human adenovirus serotype 3.
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EMBO J,
27,
956-969.
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C.J.Fang,
V.Fremeaux-Bacchi,
M.K.Liszewski,
G.Pianetti,
M.Noris,
T.H.Goodship,
and
J.P.Atkinson
(2008).
Membrane cofactor protein mutations in atypical hemolytic uremic syndrome (aHUS), fatal Stx-HUS, C3 glomerulonephritis, and the HELLP syndrome.
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Blood,
111,
624-632.
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H.Wang,
Y.Liu,
Z.Li,
S.Tuve,
D.Stone,
O.Kalyushniy,
D.Shayakhmetov,
C.L.Verlinde,
T.Stehle,
J.McVey,
A.Baker,
K.W.Peng,
S.Roffler,
and
A.Lieber
(2008).
In vitro and in vivo properties of adenovirus vectors with increased affinity to CD46.
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J Virol,
82,
10567-10579.
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L.Pache,
S.Venkataraman,
V.S.Reddy,
and
G.R.Nemerow
(2008).
Structural variations in species B adenovirus fibers impact CD46 association.
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J Virol,
82,
7923-7931.
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PDB code:
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S.Tuve,
H.Wang,
J.D.Jacobs,
R.C.Yumul,
D.F.Smith,
and
A.Lieber
(2008).
Role of cellular heparan sulfate proteoglycans in infection of human adenovirus serotype 3 and 35.
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PLoS Pathog,
4,
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H.Wang,
Y.C.Liaw,
D.Stone,
O.Kalyuzhniy,
I.Amiraslanov,
S.Tuve,
C.L.Verlinde,
D.Shayakhmetov,
T.Stehle,
S.Roffler,
and
A.Lieber
(2007).
Identification of CD46 binding sites within the adenovirus serotype 35 fiber knob.
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J Virol,
81,
12785-12792.
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PDB code:
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S.Murakami,
F.Sakurai,
K.Kawabata,
N.Okada,
T.Fujita,
A.Yamamoto,
T.Hayakawa,
and
H.Mizuguchi
(2007).
Interaction of penton base Arg-Gly-Asp motifs with integrins is crucial for adenovirus serotype 35 vector transduction in human hematopoietic cells.
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Gene Ther,
14,
1525-1533.
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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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}
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