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PDBsum entry 2wfh
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Contents |
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* Residue conservation analysis
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PDB id:
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Splicing
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Title:
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The human slit 2 dimerization domain d4
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Structure:
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Slit homolog 2 protein c-product. Chain: a, b. Fragment: dimerization domain, residues 726-907. Synonym: human slit 2 domain d4, slit-2. Engineered: yes
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Source:
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Homo sapiens. Organism_taxid: 9606. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: human embryonic kidney cells (hek 293 ebna).
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Resolution:
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1.80Å
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R-factor:
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0.186
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R-free:
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0.219
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Authors:
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E.Seiradake,A.C.Von Philipsborn,M.Henry,M.Fritz,H.Lortat-Jacob, M.Jamin,W.Hemrika,M.Bastmeyer,S.Cusack,A.A.Mccarthy
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Key ref:
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E.Seiradake
et al.
(2009).
Structure and functional relevance of the Slit2 homodimerization domain.
Embo Rep,
10,
736-741.
PubMed id:
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Date:
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06-Apr-09
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Release date:
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21-Apr-09
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PROCHECK
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Headers
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References
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O94813
(SLIT2_HUMAN) -
Slit homolog 2 protein from Homo sapiens
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Seq:
Struc:
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1529 a.a.
181 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Embo Rep
10:736-741
(2009)
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PubMed id:
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Structure and functional relevance of the Slit2 homodimerization domain.
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E.Seiradake,
A.C.von Philipsborn,
M.Henry,
M.Fritz,
H.Lortat-Jacob,
M.Jamin,
W.Hemrika,
M.Bastmeyer,
S.Cusack,
A.A.McCarthy.
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ABSTRACT
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Slit proteins are secreted ligands that interact with the Roundabout (Robo)
receptors to provide important guidance cues in neuronal and vascular
development. Slit-Robo signalling is mediated by an interaction between the
second Slit domain and the first Robo domain, as well as being dependent on
heparan sulphate. In an effort to understand the role of the other Slit domains
in signalling, we determined the crystal structure of the fourth Slit2 domain
(D4) and examined the effects of various Slit2 constructs on chick retinal
ganglion cell axons. Slit2 D4 forms a homodimer using the conserved residues on
its concave face, and can also bind to heparan sulphate. We observed that Slit2
D4 frequently results in growth cones with collapsed lamellipodia and that this
effect can be inhibited by exogenously added heparan sulphate. Our results show
that Slit2 D4-heparan sulphate binding contributes to a Slit-Robo signalling
mechanism more intricate than previously thought.
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Links
