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PDBsum entry 1bih
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Insect immunity
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PDB id
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1bih
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Contents |
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* Residue conservation analysis
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DOI no:
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Science
281:991-995
(1998)
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PubMed id:
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Crystal structure of hemolin: a horseshoe shape with implications for homophilic adhesion.
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X.D.Su,
L.N.Gastinel,
D.E.Vaughn,
I.Faye,
P.Poon,
P.J.Bjorkman.
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ABSTRACT
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Hemolin, an insect immunoglobulin superfamily member, is a
lipopolysaccharide-binding immune protein induced during bacterial infection.
The 3.1 angstrom crystal structure reveals a bound phosphate and patches of
positive charge, which may represent the lipopolysaccharide binding site, and a
new and unexpected arrangement of four immunoglobulin-like domains forming a
horseshoe. Sequence analysis and analytical ultracentrifugation suggest that the
domain arrangement is a feature of the L1 family of neural cell adhesion
molecules related to hemolin. These results are relevant to interpretation of
human L1 mutations in neurological diseases and suggest a domain swapping model
for how L1 family proteins mediate homophilic adhesion.
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Selected figure(s)
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Figure 2.
Fig. 2. (A) Sequence alignments (3, 24). Numbers refer to H.
cecropia hemolin. Locations of  -strands in
hemolin are indicated above the sequences with letter names.
Residues at the D2-D3 and D1-D4 interdomain interfaces (those
that contribute more than 10 Å2 of buried surface area to
the interfaces) are indicated with an asterisk and are green if
they are identical or chemically similar in L1 and a hemolin and
neuroglian sequence, blue if they are identical or chemically
similar in a hemolin and neuroglian sequence, and red if they
are identical or chemically similar in a hemolin and L1
sequence. Many of the highlighted residues at the D2-D3 and
D1-D4 interfaces are also conserved in axonin 1, a vertebrate
axon surface protein with which hemolin shares significant
sequence identity (28%) (7). Substituted residues in L1 mutants
(4, 5) are indicated below the L1 sequence. Hemolin's
interactions with the bound phosphate ion include the side
chains of His264, Arg153, and Tyr243, and the main-chain
nitrogens of Asn265, Arg266, Thr267, and Ser268. (B) Stereoview
of the C  backbone
of hemolin. Highlighted residues at the D2-D3 and D1-D4
interfaces [color-coded as in (A)] are identical or chemically
similar in hemolin and L1 family proteins. C atoms at
positions corresponding to pathological mutations in human L1
(4, 5) are marked with a black sphere.
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Figure 3.
Fig. 3. Schematic representation of a mechanism for
homophilic adhesion mediated by 3D domain swapping (22) in
hemolin and related proteins. On the left, the four
NH[2]-terminal domains of an L1 protein or the hemolin monomer
(color coded interfaces as in Fig. 1A) are depicted in the
closed (bent) conformation. The black line indicates the
remaining Ig-like, fibronectin type III, and transmembrane
domains in the case of the L1 proteins (4) or attachment to the
membrane by posttranslational modification in the case of
hemolin (7). Transient formation of an open form would lead to
formation of domain-swapped dimers (middle) or multimers (right)
through homophilic interactions with open proteins on another
cell. This model predicts that formation of a ribbon of
domain-swapped proteins is more likely on a membrane than in
solution: on a membrane where molecules are tethered to a
surface, a ribbon of domain-swapped proteins could be nucleated
through interactions of neighboring molecules with open
proteins, rationalizing why soluble hemolin and Nrg-4D are
monomeric (21) and soluble versions of homophilic
IgSF-containing CAMs are generally monomeric. An antiparallel
interaction of IgSF domains may be a general mechanism for
homophilic adhesion mediated by neural CAMs in addition to
proteins in the L1 family. For example, recent studies of
homophilic adhesion mediated by N-CAM are consistent with an
interaction of its five IgSF domains to create antiparallel
D1-D5, D2-D4, and D3-D3 pairs (25), resulting in N-CAM dimers or
multimers similar to those depicted in this figure.
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The above figures are
reprinted
by permission from the AAAs:
Science
(1998,
281,
991-995)
copyright 1998.
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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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B.H.Biersmith,
M.Hammel,
E.R.Geisbrecht,
and
S.Bouyain
(2011).
The Immunoglobulin-like Domains 1 and 2 of the Protein Tyrosine Phosphatase LAR Adopt an Unusual Horseshoe-like Conformation.
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J Mol Biol,
408,
616-627.
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PDB codes:
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F.Yang,
A.P.West,
and
P.J.Bjorkman
(2011).
Crystal structure of a hemojuvelin-binding fragment of neogenin at 1.8Å.
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J Struct Biol,
174,
239-244.
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PDB code:
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M.M.Chen,
C.Y.Lee,
H.A.Leland,
G.Y.Lin,
A.M.Montgomery,
and
S.Silletti
(2010).
Inside-out regulation of L1 conformation, integrin binding, proteolysis, and concomitant cell migration.
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Mol Biol Cell,
21,
1671-1685.
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O.Schmidt,
K.Söderhäll,
U.Theopold,
and
I.Faye
(2010).
Role of adhesion in arthropod immune recognition.
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Annu Rev Entomol,
55,
485-504.
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S.Bouyain,
and
D.J.Watkins
(2010).
The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members of the contactin family of neural recognition molecules.
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Proc Natl Acad Sci U S A,
107,
2443-2448.
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PDB codes:
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T.Sathaliyawala,
M.Z.Islam,
Q.Li,
A.Fokine,
M.G.Rossmann,
and
V.B.Rao
(2010).
Functional analysis of the highly antigenic outer capsid protein, Hoc, a virus decoration protein from T4-like bacteriophages.
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Mol Microbiol,
77,
444-455.
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A.Shono,
H.Tsukaguchi,
A.Kitamura,
R.Hiramoto,
X.S.Qin,
T.Doi,
and
K.Iijima
(2009).
Predisposition to relapsing nephrotic syndrome by a nephrin mutation that interferes with assembly of functioning microdomains.
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Hum Mol Genet,
18,
2943-2956.
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Y.He,
G.J.Jensen,
and
P.J.Bjorkman
(2009).
Cryo-electron tomography of homophilic adhesion mediated by the neural cell adhesion molecule L1.
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Structure,
17,
460-471.
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D.Hattori,
S.S.Millard,
W.M.Wojtowicz,
and
S.L.Zipursky
(2008).
Dscam-mediated cell recognition regulates neural circuit formation.
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Annu Rev Cell Dev Biol,
24,
597-620.
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E.Arevalo,
S.Shanmugasundararaj,
M.F.Wilkemeyer,
X.Dou,
S.Chen,
M.E.Charness,
and
K.W.Miller
(2008).
An alcohol binding site on the neural cell adhesion molecule L1.
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Proc Natl Acad Sci U S A,
105,
371-375.
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M.R.Sawaya,
W.M.Wojtowicz,
I.Andre,
B.Qian,
W.Wu,
D.Baker,
D.Eisenberg,
and
S.L.Zipursky
(2008).
A double S shape provides the structural basis for the extraordinary binding specificity of Dscam isoforms.
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Cell,
134,
1007-1018.
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PDB code:
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R.M.Gouveia,
C.M.Gomes,
M.Sousa,
P.M.Alves,
and
J.Costa
(2008).
Kinetic analysis of L1 homophilic interaction: role of the first four immunoglobulin domains and implications on binding mechanism.
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J Biol Chem,
283,
28038-28047.
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S.Marchetti,
F.Sbrana,
R.Raccis,
L.Lanzi,
C.M.Gambi,
M.Vassalli,
B.Tiribilli,
A.Pacini,
and
A.Toscano
(2008).
Dynamic light scattering and atomic force microscopy imaging on fragments of beta-connectin from human cardiac muscle.
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Phys Rev E Stat Nonlin Soft Matter Phys,
77,
021910.
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L.Shapiro,
J.Love,
and
D.R.Colman
(2007).
Adhesion molecules in the nervous system: structural insights into function and diversity.
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Annu Rev Neurosci,
30,
451-474.
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M.Mörtl,
P.Sonderegger,
K.Diederichs,
and
W.Welte
(2007).
The crystal structure of the ligand-binding module of human TAG-1 suggests a new mode of homophilic interaction.
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Protein Sci,
16,
2174-2183.
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PDB code:
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R.Meijers,
R.Puettmann-Holgado,
G.Skiniotis,
J.H.Liu,
T.Walz,
J.H.Wang,
and
D.Schmucker
(2007).
Structural basis of Dscam isoform specificity.
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Nature,
449,
487-491.
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PDB codes:
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S.Yuzawa,
Y.Opatowsky,
Z.Zhang,
V.Mandiyan,
I.Lax,
and
J.Schlessinger
(2007).
Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor.
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Cell,
130,
323-334.
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PDB codes:
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T.J.Mankelow,
N.Burton,
F.O.Stefansdottir,
F.A.Spring,
S.F.Parsons,
J.S.Pedersen,
C.L.Oliveira,
D.Lammie,
T.Wess,
N.Mohandas,
J.A.Chasis,
R.L.Brady,
and
D.J.Anstee
(2007).
The Laminin 511/521-binding site on the Lutheran blood group glycoprotein is located at the flexible junction of Ig domains 2 and 3.
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Blood,
110,
3398-3406.
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PDB codes:
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J.S.McLellan,
S.Yao,
X.Zheng,
B.V.Geisbrecht,
R.Ghirlando,
P.A.Beachy,
and
D.J.Leahy
(2006).
Structure of a heparin-dependent complex of Hedgehog and Ihog.
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Proc Natl Acad Sci U S A,
103,
17208-17213.
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PDB codes:
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M.J.Bennett,
M.R.Sawaya,
and
D.Eisenberg
(2006).
Deposition diseases and 3D domain swapping.
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Structure,
14,
811-824.
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M.Marino,
P.Zou,
D.Svergun,
P.Garcia,
C.Edlich,
B.Simon,
M.Wilmanns,
C.Muhle-Goll,
and
O.Mayans
(2006).
The Ig doublet Z1Z2: a model system for the hybrid analysis of conformational dynamics in Ig tandems from titin.
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Structure,
14,
1437-1447.
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PDB code:
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S.D.Patel,
C.Ciatto,
C.P.Chen,
F.Bahna,
M.Rajebhosale,
N.Arkus,
I.Schieren,
T.M.Jessell,
B.Honig,
S.R.Price,
and
L.Shapiro
(2006).
Type II cadherin ectodomain structures: implications for classical cadherin specificity.
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Cell,
124,
1255-1268.
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PDB codes:
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A.Carhan,
F.Allen,
J.D.Armstrong,
M.Hortsch,
S.F.Goodwin,
and
K.M.O'Dell
(2005).
Female receptivity phenotype of icebox mutants caused by a mutation in the L1-type cell adhesion molecule neuroglian.
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Genes Brain Behav,
4,
449-465.
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C.P.Chen,
S.Posy,
A.Ben-Shaul,
L.Shapiro,
and
B.H.Honig
(2005).
Specificity of cell-cell adhesion by classical cadherins: Critical role for low-affinity dimerization through beta-strand swapping.
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Proc Natl Acad Sci U S A,
102,
8531-8536.
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H.Sasakura,
H.Inada,
A.Kuhara,
E.Fusaoka,
D.Takemoto,
K.Takeuchi,
and
I.Mori
(2005).
Maintenance of neuronal positions in organized ganglia by SAX-7, a Caenorhabditis elegans homologue of L1.
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EMBO J,
24,
1477-1488.
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K.Roxström-Lindquist,
Y.Assefaw-Redda,
K.Rosinska,
and
I.Faye
(2005).
20-Hydroxyecdysone indirectly regulates Hemolin gene expression in Hyalophora cecropia.
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Insect Mol Biol,
14,
645-652.
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M.Hirai,
O.Terenius,
W.Li,
and
I.Faye
(2004).
Baculovirus and dsRNA induce Hemolin, but no antibacterial activity, in Antheraea pernyi.
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Insect Mol Biol,
13,
399-405.
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M.R.Kanost,
H.Jiang,
and
X.Q.Yu
(2004).
Innate immune responses of a lepidopteran insect, Manduca sexta.
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Immunol Rev,
198,
97.
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N.Kulahin,
C.Kasper,
M.Gajhede,
V.Berezin,
E.Bock,
and
J.S.Kastrup
(2004).
Expression, crystallization and preliminary X-ray analysis of extracellular modules of the neural cell-adhesion molecules NCAM and L1.
|
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Acta Crystallogr D Biol Crystallogr,
60,
591-593.
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A.B.Herr,
E.R.Ballister,
and
P.J.Bjorkman
(2003).
Insights into IgA-mediated immune responses from the crystal structures of human FcalphaRI and its complex with IgA1-Fc.
|
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Nature,
423,
614-620.
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PDB codes:
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A.N.Barclay
(2003).
Membrane proteins with immunoglobulin-like domains--a master superfamily of interaction molecules.
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Semin Immunol,
15,
215-223.
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B.E.Willcox,
L.M.Thomas,
T.L.Chapman,
A.P.Heikema,
A.P.West,
and
P.J.Bjorkman
(2002).
Crystal structure of LIR-2 (ILT4) at 1.8 A: differences from LIR-1 (ILT2) in regions implicated in the binding of the Human Cytomegalovirus class I MHC homolog UL18.
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BMC Struct Biol,
2,
6.
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PDB code:
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J.Jacob,
J.Haspel,
N.Kane-Goldsmith,
and
M.Grumet
(2002).
L1 mediated homophilic binding and neurite outgrowth are modulated by alternative splicing of exon 2.
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J Neurobiol,
51,
177-189.
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K.Y.Jeong,
I.Y.Lee,
H.I.Ree,
C.S.Hong,
and
T.S.Yong
(2002).
Localization of Der f 2 in the gut and fecal pellets of Dermatophagoides farinae.
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Allergy,
57,
729-731.
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V.Castellani,
E.De Angelis,
S.Kenwrick,
and
G.Rougon
(2002).
Cis and trans interactions of L1 with neuropilin-1 control axonal responses to semaphorin 3A.
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EMBO J,
21,
6348-6357.
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X.Q.Yu,
and
M.R.Kanost
(2002).
Binding of hemolin to bacterial lipopolysaccharide and lipoteichoic acid. An immunoglobulin superfamily member from insects as a pattern-recognition receptor.
|
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Eur J Biochem,
269,
1827-1834.
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C.L.Smith,
P.Khandelwal,
K.Keliikuli,
E.R.Zuiderweg,
and
M.A.Saper
(2001).
Structure of the type III secretion and substrate-binding domain of Yersinia YopH phosphatase.
|
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Mol Microbiol,
42,
967-979.
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PDB code:
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G.Schürmann,
J.Haspel,
M.Grumet,
and
H.P.Erickson
(2001).
Cell adhesion molecule L1 in folded (horseshoe) and extended conformations.
|
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Mol Biol Cell,
12,
1765-1773.
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J.Haspel,
G.Schürmann,
J.Jacob,
H.P.Erickson,
and
M.Grumet
(2001).
Disulfide-mediated dimerization of L1 Ig domains.
|
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J Neurosci Res,
66,
347-355.
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W.L.Martin,
A.P.West,
L.Gan,
and
P.J.Bjorkman
(2001).
Crystal structure at 2.8 A of an FcRn/heterodimeric Fc complex: mechanism of pH-dependent binding.
|
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Mol Cell,
7,
867-877.
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PDB codes:
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C.C.Deivanayagam,
R.L.Rich,
M.Carson,
R.T.Owens,
S.Danthuluri,
T.Bice,
M.Höök,
and
S.V.Narayana
(2000).
Novel fold and assembly of the repetitive B region of the Staphylococcus aureus collagen-binding surface protein.
|
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Structure,
8,
67-78.
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PDB codes:
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C.Wiegand,
D.Levin,
J.Gillespie,
E.Willott,
M.Kanost,
and
T.Trenczek
(2000).
Monoclonal antibody MS13 identifies a plasmatocyte membrane protein and inhibits encapsulation and spreading reactions of Manduca sexta hemocytes.
|
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Arch Insect Biochem Physiol,
45,
95.
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H.Hall,
D.Bozic,
C.Fauser,
and
J.Engel
(2000).
Trimerization of cell adhesion molecule L1 mimics clustered L1 expression on the cell surface: influence on L1-ligand interactions and on promotion of neurite outgrowth.
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J Neurochem,
75,
336-346.
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J.Freigang,
K.Proba,
L.Leder,
K.Diederichs,
P.Sonderegger,
and
W.Welte
(2000).
The crystal structure of the ligand binding module of axonin-1/TAG-1 suggests a zipper mechanism for neural cell adhesion.
|
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Cell,
101,
425-433.
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PDB code:
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J.Haspel,
D.R.Friedlander,
N.Ivgy-May,
S.Chickramane,
C.Roonprapunt,
S.Chen,
M.Schachner,
and
M.Grumet
(2000).
Critical and optimal Ig domains for promotion of neurite outgrowth by L1/Ng-CAM.
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J Neurobiol,
42,
287-302.
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S.Silletti,
F.Mei,
D.Sheppard,
and
A.M.Montgomery
(2000).
Plasmin-sensitive dibasic sequences in the third fibronectin-like domain of L1-cell adhesion molecule (CAM) facilitate homomultimerization and concomitant integrin recruitment.
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J Cell Biol,
149,
1485-1502.
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T.L.Chapman,
A.P.Heikema,
A.P.West,
and
P.J.Bjorkman
(2000).
Crystal structure and ligand binding properties of the D1D2 region of the inhibitory receptor LIR-1 (ILT2).
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Immunity,
13,
727-736.
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PDB code:
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E.De Angelis,
J.MacFarlane,
J.S.Du,
G.Yeo,
R.Hicks,
F.G.Rathjen,
S.Kenwrick,
and
T.Brümmendorf
(1999).
Pathological missense mutations of neural cell adhesion molecule L1 affect homophilic and heterophilic binding activities.
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EMBO J,
18,
4744-4753.
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R.Bettencourt,
H.Gunne,
L.Gastinel,
H.Steiner,
and
I.Faye
(1999).
Implications of hemolin glycosylation and Ca2+-binding on homophilic and cellular interactions.
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Eur J Biochem,
266,
964-976.
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X.Q.Yu,
and
M.R.Kanost
(1999).
Developmental expression of Manduca sexta hemolin.
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| |
Arch Insect Biochem Physiol,
42,
198-212.
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S.C.Garman,
J.P.Kinet,
and
T.S.Jardetzky
(1998).
Crystal structure of the human high-affinity IgE receptor.
|
| |
Cell,
95,
951-961.
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PDB code:
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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
