3RO3
crystal structure of LGN/mInscuteable complex
Summary for 3RO3
Entry DOI | 10.2210/pdb3ro3/pdb |
Related | 3RO2 |
Descriptor | G-protein-signaling modulator 2, peptide of Protein inscuteable homolog, GLYCEROL, ... (6 entities in total) |
Functional Keywords | asymmetric cell division, protein binding |
Biological source | Mus musculus (mouse) More |
Cellular location | Cytoplasm (By similarity): Q8VDU0 Cytoplasm: Q3HNM7 |
Total number of polymer chains | 2 |
Total formula weight | 21478.27 |
Authors | |
Primary citation | Zhu, 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: 21816348DOI: 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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