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3RO3

crystal structure of LGN/mInscuteable complex

Summary for 3RO3
Entry DOI10.2210/pdb3ro3/pdb
Related3RO2
DescriptorG-protein-signaling modulator 2, peptide of Protein inscuteable homolog, GLYCEROL, ... (6 entities in total)
Functional Keywordsasymmetric cell division, protein binding
Biological sourceMus musculus (mouse)
More
Cellular locationCytoplasm (By similarity): Q8VDU0
Cytoplasm: Q3HNM7
Total number of polymer chains2
Total formula weight21478.27
Authors
Zhu, J.,Wen, W.,Shang, Y.,Wei, Z.,Pan, Z.,Wang, W.,Zhang, M. (deposition date: 2011-04-25, release date: 2012-03-07, Last modification date: 2024-03-20)
Primary citationZhu, J.,Wen, W.,Zheng, Z.,Shang, Y.,Wei, Z.,Xiao, Z.,Pan, Z.,Du, Q.,Wang, W.,Zhang, M.
LGN/mInsc and LGN/NuMA complex structures suggest distinct functions in asymmetric cell division for the Par3/mInsc/LGN and G[alpha]i/LGN/NuMA pathways
Mol.Cell, 43:418-431, 2011
Cited by
PubMed Abstract: Asymmetric cell division requires the establishment of cortical cell polarity and the orientation of the mitotic spindle along the axis of cell polarity. Evidence from invertebrates demonstrates that the Par3/Par6/aPKC and NuMA/LGN/Gαi complexes, which are thought to be physically linked by the adaptor protein mInscuteable (mInsc), play indispensable roles in this process. However, the molecular basis for the binding of LGN to NuMA and mInsc is poorly understood. The high-resolution structures of the LGN/NuMA and LGN/mInsc complexes presented here provide mechanistic insights into the distinct and highly specific interactions of the LGN TPRs with mInsc and NuMA. Structural comparisons, together with biochemical and cell biology studies, demonstrate that the interactions of NuMA and mInsc with LGN are mutually exclusive, with mInsc binding preferentially. Our results suggest that the Par3/mInsc/LGN and NuMA/LGN/Gαi complexes play sequential and partially overlapping roles in asymmetric cell division.
PubMed: 21816348
DOI: 10.1016/j.molcel.2011.07.011
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.1 Å)
Structure validation

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数据于2024-10-30公开中

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