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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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PDB id:
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| Name: |
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Signaling protein
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Title:
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An auto-inhibited conformation of lgn reveals a distinct interaction mode between goloco motifs and tpr motifs
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Structure:
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G-protein-signaling modulator 2. Chain: a, b. Synonym: pins homolog. Engineered: yes
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Gene: gpsm2, lgn, pins. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.80Å
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R-factor:
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0.253
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R-free:
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0.311
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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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Key ref:
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Z.Pan
et al.
(2013).
An autoinhibited conformation of LGN reveals a distinct interaction mode between GoLoco motifs and TPR motifs.
Structure,
21,
1007-1017.
PubMed id:
DOI:
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Date:
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05-Mar-13
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Release date:
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05-Jun-13
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PROCHECK
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Headers
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References
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Q8VDU0
(GPSM2_MOUSE) -
G-protein-signaling modulator 2 from Mus musculus
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Seq:
Struc:
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679 a.a.
290 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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*
PDB and UniProt seqs differ
at 59 residue positions (black
crosses)
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DOI no:
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Structure
21:1007-1017
(2013)
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PubMed id:
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An autoinhibited conformation of LGN reveals a distinct interaction mode between GoLoco motifs and TPR motifs.
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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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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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Links
