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PDBsum entry 2wfh
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References listed in PDB file
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Key reference
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Title
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Structure and functional relevance of the slit2 homodimerization domain.
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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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Ref.
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Embo Rep, 2009,
10,
736-741.
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PubMed id
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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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