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PDBsum entry 4jhr
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Signaling protein
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PDB id
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4jhr
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References listed in PDB file
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Key reference
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Title
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An autoinhibited conformation of lgn reveals a distinct interaction mode between goloco motifs and tpr motifs.
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Authors
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Z.Pan,
J.Zhu,
Y.Shang,
Z.Wei,
M.Jia,
C.Xia,
W.Wen,
W.Wang,
M.Zhang.
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Ref.
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Structure, 2013,
21,
1007-1017.
[DOI no: ]
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PubMed id
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Abstract
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LGN plays essential roles in asymmetric cell divisions via its N-terminal
TPR-motif-mediated binding to mInsc and NuMA. This scaffolding activity requires
the release of the autoinhibited conformation of LGN by binding of Gα(i) to its
C-terminal GoLoco (GL) motifs. The interaction between the GL and TPR motifs of
LGN represents a distinct GL/target binding mode with an unknown mechanism.
Here, we show that two consecutive GL motifs of LGN form a minimal
TPR-motif-binding unit. GL12 and GL34 bind to TPR0-3 and TPR4-7, respectively.
The crystal structure of a truncated LGN reveals that GL34 forms a pair of
parallel α helices and binds to the concave surface of TPR4-7, thereby
preventing LGN from binding to other targets. Importantly, the GLs bind to TPR
motifs with a mode distinct from that observed in the GL/Gα(i)·GDP complexes.
Our results also indicate that multiple and orphan GL motif proteins likely
respond to G proteins with distinct mechanisms.
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