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PDBsum entry 4rtt
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Protein binding
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PDB id
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4rtt
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References listed in PDB file
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Key reference
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Title
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The neuronal migration factor srgap2 achieves specificity in ligand binding through a two-Component molecular mechanism.
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Authors
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J.Guez-Haddad,
M.Sporny,
Y.Sasson,
L.Gevorkyan-Airapetov,
N.Lahav-Mankovski,
D.Margulies,
J.Radzimanowski,
Y.Opatowsky.
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Ref.
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Structure, 2015,
23,
1989-2000.
[DOI no: ]
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PubMed id
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Abstract
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srGAP proteins regulate cell migration and morphogenesis by shaping the
structure and dynamics of the cytoskeleton and membranes. First discovered as
intracellular effectors for the Robo1 axon-guidance receptor, srGAPs were later
identified as interacting with several other nuclear and cytoplasmic proteins.
In all these cases, the srGAP SH3 domain mediates protein-protein interactions
by recognizing a short proline-rich segment on the cognate-binding partner.
However, as interactions between the isolated SH3 domain and a selected set of
ligands show weak affinity and low specificity, it is not clear how srGAPs are
precisely recruited to their signaling sites. Here, we report a two-component
molecular mechanism that regulates ligand binding to srGAP2 by on the one hand
dramatically tightening their association and on the other, moderately
autoinhibiting and restricting binding. Our results allow the design of point
mutations for better probing of srGAP2 activities, and may facilitate the
identification of new srGAP2 ligands.
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