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PDBsum entry 5fjy
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Protein transport
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PDB id
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5fjy
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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 light chains of kinesin-1 are autoinhibited.
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Authors
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Y.Y.Yip,
S.Pernigo,
A.Sanger,
M.Xu,
M.Parsons,
R.A.Steiner,
M.P.Dodding.
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Ref.
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Proc Natl Acad Sci U S A, 2016,
113,
2418-2423.
[DOI no: ]
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PubMed id
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Abstract
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The light chains (KLCs) of the microtubule motor kinesin-1 bind cargoes and
regulate its activity. Through their tetratricopeptide repeat domain (KLC(TPR)),
they can recognize short linear peptide motifs found in many cargo proteins
characterized by a central tryptophan flanked by aspartic/glutamic acid residues
(W-acidic). Using a fluorescence resonance energy transfer biosensor in
combination with X-ray crystallographic, biochemical, and biophysical
approaches, we describe how an intramolecular interaction between the KLC2(TPR)
domain and a conserved peptide motif within an unstructured region of the
molecule, partly occludes the W-acidic binding site on the TPR domain. Cargo
binding displaces this interaction, effecting a global conformational change in
KLCs resulting in a more extended conformation. Thus, like the motor-bearing
kinesin heavy chains, KLCs exist in a dynamic conformational state that is
regulated by self-interaction and cargo binding. We propose a model by which,
via this molecular switch, W-acidic cargo binding regulates the activity of the
holoenzyme.
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Secondary reference #1
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Title
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Structural basis for kinesin-1:cargo recognition.
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Authors
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S.Pernigo,
A.Lamprecht,
R.A.Steiner,
M.P.Dodding.
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Ref.
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Science, 2013,
340,
356-359.
[DOI no: ]
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PubMed id
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