3RO2: LGN/NuMA complex

Structures of the LGN/NuMA complex. Determined by X-ray diffraction at 2.3 Å resolution. Released 7 Mar 2012.

Method: X-ray diffraction
Resolution: 2.3 Å
Organisms: Mus musculus, Homo sapiens
Chains: 2
Atoms: 2,792
Mol. weight: 41.07 kDa
Released: 7 Mar 2012

Explore 3RO2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3RO2 contains 18 α-helices and 0 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 16 helices, 0 β-strands

Element	Residues	Length
α-helix	14-29	16
α-helix	33-46	14
α-helix	51-67	17
α-helix	71-88	18
α-helix	91-107	17
α-helix	111-127	17
α-helix	131-150	20
α-helix	165-188	24
α-helix	191-208	18
α-helix	211-228	18
α-helix	231-248	18
α-helix	251-267	17
α-helix	271-287	17
α-helix	291-308	18
α-helix	311-328	18
α-helix	331-343	13

Chain B: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	1999-2002	4
α-helix	2010-2012	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
G-protein-signaling modulator 2	A	protein	338	Mus musculus	Q8VDU0 (AlphaFold model)
peptide of Nuclear mitotic apparatus protein 1	B	protein	28	Homo sapiens	Q14980 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3RO2_1 G-protein-signaling modulator 2 (chains A)
GSASCLELALEGERLCKSGDCRAGVSFFEAAVQVGTEDLKTLSAIYSQLGNAYFYLHDYA
KALEYHHHDLTLARTIGDQLGEAKASGNLGNTLKVLGNFDEAIVCCQRHLDISRELNDKV
GEARALYNLGNVYHAKGKSFGCPGPQDTGEFPEDVRNALQAAVDLYEENLSLVTALGDRA
AQGRAFGNLGNTHYLLGNFRDAVIAHEQRLLIAKEFGDKAAERRAYSNLGNAYIFLGEFE
TASEYYKKTLLLARQLKDRAVEAQSCYSLGNTYTLLQDYEKAIDYHLKHLAIAQELKDRI
GEGRACWSLGNAYTALGNHDQAMHFAEKHLEISREVGD

Sequence of entity 2 (B), FASTA

>3RO2_2 peptide of Nuclear mitotic apparatus protein 1 (chains B)
RNSFYMGTCQDEPEQLDDWNRIAELQQR

Primary citation

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. Zhu, J., Wen, W., Zheng, Z. et al. Mol Cell (2011) 43:418-431. DOI 10.1016/j.molcel.2011.07.011 · PubMed

Other PDB entries of the same protein (UniProt Q8VDU0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3RO3 1.1 Å, crystal structure of LGN/mInscuteable complex
4G2V 2.4 Å, Structure complex of LGN binding with FRMPD1
7EP7 2.6 Å, The complex structure of Gpsm2 and Whirlin
4JHR 2.8 Å, An auto-inhibited conformation of LGN reveals a distinct interaction mode between GoLoco…
4G5O 2.9 Å, Structure of LGN GL4/Galphai3(Q147L) complex
4G5Q 2.9 Å, Structure of LGN GL4/Galphai1 complex
4G5R 3.48 Å, Structure of LGN GL4/Galphai3 complex
4G5S 3.62 Å, Structure of LGN GL3/Galphai3 complex

Browse structure collections

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