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Contents |
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* Residue conservation analysis
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Enzyme class:
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Chains B, D:
E.C.2.7.10.1
- receptor protein-tyrosine kinase.
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Reaction:
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L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H+
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L-tyrosyl-[protein]
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+
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ATP
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=
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O-phospho-L-tyrosyl-[protein]
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+
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ADP
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Nature
407:1029-1034
(2000)
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PubMed id:
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Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin.
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L.Pellegrini,
D.F.Burke,
F.von Delft,
B.Mulloy,
T.L.Blundell.
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ABSTRACT
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Fibroblast growth factors (FGFs) are a large family of structurally related
proteins with a wide range of physiological and pathological activities. Signal
transduction requires association of FGF with its receptor tyrosine kinase
(FGFR) and heparan sulphate proteoglycan in a specific complex on the cell
surface. Direct involvement of the heparan sulphate glycosaminoglycan
polysaccharide in the molecular association between FGF and its receptor is
essential for biological activity. Although crystal structures of binary
complexes of FGF-heparin and FGF-FGFR have been described, the molecular
architecture of the FGF signalling complex has not been elucidated. Here we
report the crystal structure of the FGFR2 ectodomain in a dimeric form that is
induced by simultaneous binding to FGF1 and a heparin decasaccharide. The
complex is assembled around a central heparin molecule linking two FGF1 ligands
into a dimer that bridges between two receptor chains. The asymmetric heparin
binding involves contacts with both FGF1 molecules but only one receptor chain.
The structure of the FGF1-FGFR2-heparin ternary complex provides a structural
basis for the essential role of heparan sulphate in FGF signalling.
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Selected figure(s)
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Figure 1.
Figure 1: The FGF1-FGFR2-heparin complex. a, View
perpendicular to the approximate dyad of the complex. FGFR2
domains 2 (D2) and 3 (D3) are cyan and magenta, respectively,
and FGF1 is green. The heparin molecule is in CPK
representation. b, View along the dyad. c, Amino-acid sequence
of the ligand-binding region of human FGFR2. Domains D2 and D3
are coloured as in a. Residues that interact with heparin and
FGF1 are highlighted in red and green, respectively. Regions of
secondary structure are boxed.  -strands,
 -helices
and 3[ 10] helices are indicated below the relative sequence. D3
residues 294-309, which were disordered in the crystals, are in
lower case.
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Figure 3.
Figure 3: Overall architecture of the FGF1-FGFR2-heparin
complex. a, Electrostatic potential of the heparin-binding
site in the FGF1-FGFR2-heparin complex, mapped onto a molecular
surface rendition of the complex. The heparin is shown as a
stick model. In the ternary complex, the heparin decasaccharide
is surrounded by regions of positive charge (blue represents
+20e per Å 2). b, Superposition of heparin-linked FGF1 dimers.
The dimer from the FGF1-FGFR2-heparin complex is yellow, the PDB
entry 2AXM is blue. The FGFR2 ectodomains are shown in CPK
representation.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2000,
407,
1029-1034)
copyright 2000.
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Figures were
selected
by an automated process.
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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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PDB code:
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Heparan sulfate acts as a bone morphogenetic protein coreceptor by facilitating ligand-induced receptor hetero-oligomerization.
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Mol Biol Cell,
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IUBMB Life,
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J Biol Chem,
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J.Moreaux,
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APRIL and TACI interact with syndecan-1 on the surface of multiple myeloma cells to form an essential survival loop.
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Increased protein stability of FGF1 can compensate for its reduced affinity for heparin.
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and
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Interactions of hepatocyte growth factor/scatter factor with various glycosaminoglycans reveal an important interplay between the presence of iduronate and sulfate density.
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J Biol Chem,
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Heparin-induced cis- and trans-dimerization modes of the thrombospondin-1 N-terminal domain.
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J Biol Chem,
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PDB codes:
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M.E.Levenstein,
W.T.Berggren,
J.E.Lee,
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Secreted proteoglycans directly mediate human embryonic stem cell-basic fibroblast growth factor 2 interactions critical for proliferation.
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Structural and functional analysis of slit and heparin binding to immunoglobulin-like domains 1 and 2 of Drosophila Robo.
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J Biol Chem,
283,
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PDB codes:
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N.Kulahin,
V.Kiselyov,
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J.S.Kastrup,
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E.Bock,
and
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Dimerization effect of sucrose octasulfate on rat FGF1.
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PDB code:
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N.S.Gandhi,
and
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and
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Evidence that heparin saccharides promote FGF2 mitogenesis through two distinct mechanisms.
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and
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Direct binding of integrin alphavbeta3 to FGF1 plays a role in FGF1 signaling.
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J Biol Chem,
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and
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Specific heparan sulfate structures modulate FGF10-mediated submandibular gland epithelial morphogenesis and differentiation.
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W.Zhang,
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Effect of FGF-binding Protein 3 on Vascular Permeability.
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J Biol Chem,
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Proc Natl Acad Sci U S A,
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PDB codes:
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C.R.Holst,
H.Bou-Reslan,
B.B.Gore,
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PLoS ONE,
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Profiling the sulfation specificities of glycosaminoglycan interactions with growth factors and chemotactic proteins using microarrays.
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Chem Biol,
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Src kinase modulates the activation, transport and signalling dynamics of fibroblast growth factor receptors.
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| |
EMBO Rep,
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J.Jacobs
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| |
Drug Discov Today,
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|
J.L.de Paz,
C.Noti,
F.Böhm,
S.Werner,
and
P.H.Seeberger
(2007).
Potentiation of fibroblast growth factor activity by synthetic heparin oligosaccharide glycodendrimers.
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| |
Chem Biol,
14,
879-887.
|
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|
|
|
|
K.Park,
Y.S.Kim,
G.Y.Lee,
J.O.Nam,
S.K.Lee,
R.W.Park,
S.Y.Kim,
I.S.Kim,
and
Y.Byun
(2007).
Antiangiogenic effect of bile acid acylated heparin derivative.
|
| |
Pharm Res,
24,
176-185.
|
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|
|
|
|
|
N.Kulahin,
V.Kiselyov,
A.Kochoyan,
O.Kristensen,
J.S.Kastrup,
V.Berezin,
E.Bock,
and
M.Gajhede
(2007).
Structure of rat acidic fibroblast growth factor at 1.4 A resolution.
|
| |
Acta Crystallogr Sect F Struct Biol Cryst Commun,
63,
65-68.
|
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PDB code:
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N.Salamat-Miller,
J.Fang,
C.W.Seidel,
Y.Assenov,
M.Albrecht,
and
C.R.Middaugh
(2007).
A network-based analysis of polyanion-binding proteins utilizing human protein arrays.
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| |
J Biol Chem,
282,
10153-10163.
|
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|
P.M.Smallwood,
J.Williams,
Q.Xu,
D.J.Leahy,
and
J.Nathans
(2007).
Mutational analysis of Norrin-Frizzled4 recognition.
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| |
J Biol Chem,
282,
4057-4068.
|
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The N-terminal domain of hepatocyte growth factor inhibits the angiogenic behavior of endothelial cells independently from binding to the c-met receptor.
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J Biol Chem,
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The involvement of heparan sulfate (HS) in FGF1/HS/FGFR1 signaling complex.
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J Biol Chem,
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Fibroblast growth factor receptors 1 and 2 interact differently with heparin/heparan sulfate. Implications for dynamic assembly of a ternary signaling complex.
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J Biol Chem,
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FGFs, their receptors, and human limb malformations: clinical and molecular correlations.
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Am J Med Genet,
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Structural basis for activation of fibroblast growth factor signaling by sucrose octasulfate.
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Mol Cell Biol,
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B.M.Loo,
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Heparin/Heparan sulfate domains in binding and signaling of fibroblast growth factor 8b.
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J Biol Chem,
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C.Mundhenke,
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Heparan sulfate proteoglycans as regulators of fibroblast growth factor-2 receptor binding in breast carcinomas.
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Am J Pathol,
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J Biol Chem,
277,
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D.G.Vanselow
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Role of constraint in catalysis and high-affinity binding by proteins.
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Biophys J,
82,
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D.McCabe,
T.Cukierman,
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Basic residues in azurocidin/HBP contribute to both heparin binding and antimicrobial activity.
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J Biol Chem,
277,
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H.Ogiso,
R.Ishitani,
O.Nureki,
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M.Yamanaka,
J.H.Kim,
K.Saito,
A.Sakamoto,
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M.Shirouzu,
and
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(2002).
Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.
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Cell,
110,
775-787.
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PDB code:
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I.Capila,
and
R.J.Linhardt
(2002).
Heparin-protein interactions.
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Angew Chem Int Ed Engl,
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J.D.Esko,
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(2002).
Order out of chaos: assembly of ligand binding sites in heparan sulfate.
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Annu Rev Biochem,
71,
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J.Kim,
S.I.Blaber,
and
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(2002).
Alternative type I and I' turn conformations in the beta8/beta9 beta-hairpin of human acidic fibroblast growth factor.
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Protein Sci,
11,
459-466.
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PDB codes:
|
|
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|
|
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|
|
J.Kreuger,
T.Matsumoto,
M.Vanwildemeersch,
T.Sasaki,
R.Timpl,
L.Claesson-Welsh,
D.Spillmann,
and
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(2002).
Role of heparan sulfate domain organization in endostatin inhibition of endothelial cell function.
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EMBO J,
21,
6303-6311.
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J.M.Trowbridge,
J.A.Rudisill,
D.Ron,
and
R.L.Gallo
(2002).
Dermatan sulfate binds and potentiates activity of keratinocyte growth factor (FGF-7).
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J Biol Chem,
277,
42815-42820.
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K.Tan,
M.Duquette,
J.H.Liu,
Y.Dong,
R.Zhang,
A.Joachimiak,
J.Lawler,
and
J.H.Wang
(2002).
Crystal structure of the TSP-1 type 1 repeats: a novel layered fold and its biological implication.
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J Cell Biol,
159,
373-382.
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PDB code:
|
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|
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|
|
P.F.Varela,
A.S.Llera,
R.A.Mariuzza,
and
J.Tormo
(2002).
Crystal structure of imaginal disc growth factor-2. A member of a new family of growth-promoting glycoproteins from Drosophila melanogaster.
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J Biol Chem,
277,
13229-13236.
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PDB codes:
|
|
|
|
|
|
|
|
S.H.Kan,
N.Elanko,
D.Johnson,
L.Cornejo-Roldan,
J.Cook,
E.W.Reich,
S.Tomkins,
A.Verloes,
S.R.Twigg,
S.Rannan-Eliya,
D.M.McDonald-McGinn,
E.H.Zackai,
S.A.Wall,
M.Muenke,
and
A.O.Wilkie
(2002).
Genomic screening of fibroblast growth-factor receptor 2 reveals a wide spectrum of mutations in patients with syndromic craniosynostosis.
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Am J Hum Genet,
70,
472-486.
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S.M.Prince,
M.Achtman,
and
J.P.Derrick
(2002).
Crystal structure of the OpcA integral membrane adhesin from Neisseria meningitidis.
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| |
Proc Natl Acad Sci U S A,
99,
3417-3421.
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PDB code:
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|
|
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T.L.Blundell,
H.Jhoti,
and
C.Abell
(2002).
High-throughput crystallography for lead discovery in drug design.
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Nat Rev Drug Discov,
1,
45-54.
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T.P.Garrett,
N.M.McKern,
M.Lou,
T.C.Elleman,
T.E.Adams,
G.O.Lovrecz,
H.J.Zhu,
F.Walker,
M.J.Frenkel,
P.A.Hoyne,
R.N.Jorissen,
E.C.Nice,
A.W.Burgess,
and
C.W.Ward
(2002).
Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha.
|
| |
Cell,
110,
763-773.
|
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|
PDB code:
|
|
|
|
|
|
|
|
T.Sasaki,
P.G.Knyazev,
Y.Cheburkin,
W.Göhring,
D.Tisi,
A.Ullrich,
R.Timpl,
and
E.Hohenester
(2002).
Crystal structure of a C-terminal fragment of growth arrest-specific protein Gas6. Receptor tyrosine kinase activation by laminin G-like domains.
|
| |
J Biol Chem,
277,
44164-44170.
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PDB code:
|
|
|
|
|
|
|
|
B.L.Allen,
M.S.Filla,
and
A.C.Rapraeger
(2001).
Role of heparan sulfate as a tissue-specific regulator of FGF-4 and FGF receptor recognition.
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| |
J Cell Biol,
155,
845-858.
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B.Mulloy,
and
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(2001).
Order out of complexity--protein structures that interact with heparin.
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Curr Opin Struct Biol,
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C.W.Mandl,
H.Kroschewski,
S.L.Allison,
R.Kofler,
H.Holzmann,
T.Meixner,
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Adaptation of tick-borne encephalitis virus to BHK-21 cells results in the formation of multiple heparan sulfate binding sites in the envelope protein and attenuation in vivo.
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| |
J Virol,
75,
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D.Lietha,
D.Y.Chirgadze,
B.Mulloy,
T.L.Blundell,
and
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(2001).
Crystal structures of NK1-heparin complexes reveal the basis for NK1 activity and enable engineering of potent agonists of the MET receptor.
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| |
EMBO J,
20,
5543-5555.
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PDB codes:
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G.J.Strewler
(2001).
FGF23, hypophosphatemia, and rickets: has phosphatonin been found?
|
| |
Proc Natl Acad Sci U S A,
98,
5945-5946.
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H.J.Hecht,
R.Adar,
B.Hofmann,
O.Bogin,
H.Weich,
and
A.Yayon
(2001).
Structure of fibroblast growth factor 9 shows a symmetric dimer with unique receptor- and heparin-binding interfaces.
|
| |
Acta Crystallogr D Biol Crystallogr,
57,
378-384.
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|
PDB code:
|
|
|
|
|
|
|
|
J.D.Esko,
and
U.Lindahl
(2001).
Molecular diversity of heparan sulfate.
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J Clin Invest,
108,
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J.T.Gallagher
(2001).
Heparan sulfate: growth control with a restricted sequence menu.
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J Clin Invest,
108,
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Heparan sulfate: decoding a dynamic multifunctional cell regulator.
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Trends Cell Biol,
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L.Pellegrini
(2001).
Role of heparan sulfate in fibroblast growth factor signalling: a structural view.
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Curr Opin Struct Biol,
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O.A.Ibrahimi,
A.V.Eliseenkova,
A.N.Plotnikov,
K.Yu,
D.M.Ornitz,
and
M.Mohammadi
(2001).
Structural basis for fibroblast growth factor receptor 2 activation in Apert syndrome.
|
| |
Proc Natl Acad Sci U S A,
98,
7182-7187.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
P.Bellosta,
A.Iwahori,
A.N.Plotnikov,
A.V.Eliseenkova,
C.Basilico,
and
M.Mohammadi
(2001).
Identification of receptor and heparin binding sites in fibroblast growth factor 4 by structure-based mutagenesis.
|
| |
Mol Cell Biol,
21,
5946-5957.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
R.V.Iozzo,
and
J.D.San Antonio
(2001).
Heparan sulfate proteoglycans: heavy hitters in the angiogenesis arena.
|
| |
J Clin Invest,
108,
349-355.
|
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Z.Zhang,
C.Coomans,
and
G.David
(2001).
Membrane heparan sulfate proteoglycan-supported FGF2-FGFR1 signaling: evidence in support of the "cooperative end structures" model.
|
| |
J Biol Chem,
276,
41921-41929.
|
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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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