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PDBsum entry 1dv8
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Signaling protein
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PDB id
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1dv8
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Contents |
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* Residue conservation analysis
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DOI no:
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J Mol Biol
300:857-865
(2000)
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PubMed id:
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Crystal structure of the carbohydrate recognition domain of the H1 subunit of the asialoglycoprotein receptor.
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M.Meier,
M.D.Bider,
V.N.Malashkevich,
M.Spiess,
P.Burkhard.
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ABSTRACT
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The human asialoglycoprotein receptor (ASGPR), also called hepatic lectin, is an
integral membrane protein and is responsible for the clearance of desialylated,
galactose-terminal glycoproteins from the circulation by receptor-mediated
endocytosis. It can be subdivided into four functional domains: the cytosolic
domain, the transmembrane domain, the stalk and the carbohydrate recognition
domain (CRD). The galactose-binding domains belong to the superfamily of C-type
(calcium-dependent) lectins, in particular to the long-form subfamily with three
conserved intramolecular disulphide bonds. It is able to bind terminal
non-reducing galactose residues and N-acetyl-galactosamine residues of
desialated tri or tetra-antennary N-linked glycans. The ASGPR is a potential
liver-specific receptor for hepatitis B virus and Marburg virus and has been
used to target exogenous molecules specifically to hepatocytes for diagnostic
and therapeutic purposes.Here, we present the X-ray crystal structure of the
carbohydrate recognition domain of the major subunit H1 at 2.3 A resolution.
While the overall fold of this and other known C-type lectin structures are well
conserved, the positions of the bound calcium ions are not, indicating that the
fold is stabilised by alternative mechanisms in different branches of the C-type
lectin family. It is the first CRD structure where three calcium ions form an
intergral part of the structure. In addition, the structure provides direct
confirmation for the conversion of the ligand-binding site of the
mannose-binding protein to an asialoglycoprotein receptor-like specificity
suggested by Drickamer and colleagues. In agreement with the prediction that the
coiled-coil domain of the ASGPR is separated from the CRD and its N-terminal
disulphide bridge by several residues, these residues are indeed not
alpha-helical, while in tetranectin they form an alpha-helical coiled-coil.
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Selected figure(s)
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Figure 1.
Figure 1. Ribbon diagram of the H1-CRD. The two a-helices are shown in magenta, the b-strands in blue, the cal-
cium ions in green and the three disulphide bridges in yellow. Both the N and the C terminus are on the bottom of
the image. The division of the structure into two subdomains can be seen. Note the sharp bend in b-strand 3. The
sugar binds to calcium ion 2 in front of the glycine-rich loop in the upper part of the picture (marked by a black
arrow). All Figures were drawn using the program DINO (Philippsen, 1999: http://www.bioz.unibas.ch/~xray/
dino).
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Figure 3.
Figure 3. Overlay of the sugar-binding site of the H1-CRD of the ASGPR (grey) and the CRD of the QPDWGH
mutant of the MBP (brown) containing an N-acetyl galactosamine (NGA) molecule as ligand (green). An omit map of
the water molecules of the H1-CRD is shown contoured at a s-level of 3.5 (red).
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2000,
300,
857-865)
copyright 2000.
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Figures were
selected
by the author.
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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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B.Hu,
Y.Yang,
J.Liu,
Z.Ma,
H.Huang,
S.Liu,
Y.Yu,
Y.Hao,
B.Wang,
M.Lu,
and
D.Yang
(2010).
Establishment of a functional cell line expressing both subunits of H1a and H2c of human hepatocyte surface molecule ASGPR.
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J Huazhong Univ Sci Technolog Med Sci,
30,
556-561.
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I.Massarelli,
F.Chiellini,
E.Chiellini,
and
A.M.Bianucci
(2010).
Three-Dimensional Models of the Oligomeric Human Asialoglycoprotein Receptor (ASGP-R).
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Int J Mol Sci,
11,
3867-3884.
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J.Diao,
and
E.Tajkhorshid
(2008).
Indirect role of Ca2+ in the assembly of extracellular matrix proteins.
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Biophys J,
95,
120-127.
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M.Sakakura,
S.Oo-Puthinan,
C.Moriyama,
T.Kimura,
J.Moriya,
T.Irimura,
and
I.Shimada
(2008).
Carbohydrate binding mechanism of the macrophage galactose-type C-type lectin 1 revealed by saturation transfer experiments.
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J Biol Chem,
283,
33665-33673.
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G.Gupta,
and
A.Surolia
(2007).
Collectins: sentinels of innate immunity.
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Bioessays,
29,
452-464.
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H.Feinberg,
M.E.Taylor,
and
W.I.Weis
(2007).
Scavenger receptor C-type lectin binds to the leukocyte cell surface glycan Lewis(x) by a novel mechanism.
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J Biol Chem,
282,
17250-17258.
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PDB codes:
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J.Brown,
C.A.O'Callaghan,
A.S.Marshall,
R.J.Gilbert,
C.Siebold,
S.Gordon,
G.D.Brown,
and
E.Y.Jones
(2007).
Structure of the fungal beta-glucan-binding immune receptor dectin-1: implications for function.
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Protein Sci,
16,
1042-1052.
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PDB codes:
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Y.Yang,
H.Huang,
Z.Zhang,
B.Wang,
Y.Tian,
M.Lu,
and
D.Yang
(2007).
Cloning, expression and polyclonal antibody preparation of the asialoglycoprotein receptor of Marmota Himalayan.
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J Huazhong Univ Sci Technolog Med Sci,
27,
411-414.
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B.A.Wurzburg,
S.S.Tarchevskaya,
and
T.S.Jardetzky
(2006).
Structural changes in the lectin domain of CD23, the low-affinity IgE receptor, upon calcium binding.
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Structure,
14,
1049-1058.
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PDB codes:
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J.H.Park,
K.L.Kim,
and
E.W.Cho
(2006).
Detection of surface asialoglycoprotein receptor expression in hepatic and extra-hepatic cells using a novel monoclonal antibody.
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Biotechnol Lett,
28,
1061-1069.
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M.I.Prata,
A.C.Santos,
S.Torres,
J.P.André,
J.A.Martins,
M.Neves,
M.L.García-Martín,
T.B.Rodrigues,
P.López-Larrubia,
S.Cerdán,
and
C.F.Geraldes
(2006).
Targeting of lanthanide(III) chelates of DOTA-type glycoconjugates to the hepatic asyaloglycoprotein receptor: cell internalization and animal imaging studies.
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Contrast Media Mol Imaging,
1,
246-258.
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A.N.Zelensky,
and
J.E.Gready
(2005).
The C-type lectin-like domain superfamily.
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FEBS J,
272,
6179-6217.
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M.Ambrosi,
N.R.Cameron,
and
B.G.Davis
(2005).
Lectins: tools for the molecular understanding of the glycocode.
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Org Biomol Chem,
3,
1593-1608.
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A.Lundell,
A.I.Olin,
M.Mörgelin,
S.al-Karadaghi,
A.Aspberg,
and
D.T.Logan
(2004).
Structural basis for interactions between tenascins and lectican C-type lectin domains: evidence for a crosslinking role for tenascins.
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Structure,
12,
1495-1506.
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PDB code:
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E.I.Park,
and
J.U.Baenziger
(2004).
Closely related mammals have distinct asialoglycoprotein receptor carbohydrate specificities.
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J Biol Chem,
279,
40954-40959.
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J.K.van de Wetering,
L.M.van Golde,
and
J.J.Batenburg
(2004).
Collectins: players of the innate immune system.
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Eur J Biochem,
271,
1229-1249.
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A.N.Zelensky,
and
J.E.Gready
(2003).
Comparative analysis of structural properties of the C-type-lectin-like domain (CTLD).
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Proteins,
52,
466-477.
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B.Saunier,
M.Triyatni,
L.Ulianich,
P.Maruvada,
P.Yen,
and
L.D.Kohn
(2003).
Role of the asialoglycoprotein receptor in binding and entry of hepatitis C virus structural proteins in cultured human hepatocytes.
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J Virol,
77,
546-559.
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E.I.Park,
S.M.Manzella,
and
J.U.Baenziger
(2003).
Rapid clearance of sialylated glycoproteins by the asialoglycoprotein receptor.
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J Biol Chem,
278,
4597-4602.
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G.Lin,
G.Simmons,
S.Pöhlmann,
F.Baribaud,
H.Ni,
G.J.Leslie,
B.S.Haggarty,
P.Bates,
D.Weissman,
J.A.Hoxie,
and
R.W.Doms
(2003).
Differential N-linked glycosylation of human immunodeficiency virus and Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and DC-SIGNR.
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J Virol,
77,
1337-1346.
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M.Triyatni,
B.Saunier,
P.Maruvada,
A.R.Davis,
L.Ulianich,
T.Heller,
A.Patel,
L.D.Kohn,
and
T.J.Liang
(2002).
Interaction of hepatitis C virus-like particles and cells: a model system for studying viral binding and entry.
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J Virol,
76,
9335-9344.
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M.Tsuiji,
M.Fujimori,
Y.Ohashi,
N.Higashi,
T.M.Onami,
S.M.Hedrick,
and
T.Irimura
(2002).
Molecular cloning and characterization of a novel mouse macrophage C-type lectin, mMGL2, which has a distinct carbohydrate specificity from mMGL1.
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J Biol Chem,
277,
28892-28901.
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T.B.Geijtenbeek,
G.C.van Duijnhoven,
S.J.van Vliet,
E.Krieger,
G.Vriend,
C.G.Figdor,
and
Y.van Kooyk
(2002).
Identification of different binding sites in the dendritic cell-specific receptor DC-SIGN for intercellular adhesion molecule 3 and HIV-1.
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J Biol Chem,
277,
11314-11320.
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T.Hatakeyama,
N.Matsuo,
K.Shiba,
S.Nishinohara,
N.Yamasaki,
H.Sugawara,
and
H.Aoyagi
(2002).
Amino acid sequence and carbohydrate-binding analysis of the N-acetyl-D-galactosamine-specific C-type lectin, CEL-I, from the Holothuroidea, Cucumaria echinata.
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Biosci Biotechnol Biochem,
66,
157-163.
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H.Kogelberg,
and
T.Feizi
(2001).
New structural insights into lectin-type proteins of the immune system.
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Curr Opin Struct Biol,
11,
635-643.
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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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Links
