3W6R

Crystal structure of the GAP domain of human MgcRacGAP

Summary for 3W6R

Entry DOI	10.2210/pdb3w6r/pdb
Descriptor	Rac GTPase-activating protein 1 (2 entities in total)
Functional Keywords	gtpase activating, signaling protein
Biological source	Homo sapiens (human)
Cellular location	Nucleus: Q9H0H5
Total number of polymer chains	1
Total formula weight	22788.62
Authors	Matsuura, A.,Lee, H.H. (deposition date: 2013-02-21, release date: 2014-02-26, Last modification date: 2023-11-08)
Primary citation	Matsuura, A.,Lee, H.H. Crystal structure of GTPase-activating domain from human MgcRacGAP. Biochem.Biophys.Res.Commun., 435:367-372, 2013 Cited by PubMed Abstract: Cytokinesis in animal cells relies on a centralspindlin complex consisting of male germ cell RacGap (MgcRacGAP) and mitotic kinesin-like protein 1 (MKLP1). Rho GTPases act as molecular switches to regulate the actin cytoskeleton for cytokinesis, of which Rac1 is regulated by MgcRacGAP. In this study, we determined the crystal structure of the GTPase-activating protein (GAP) domain of MgcRacGAP at a resolution of 1.9Å. The conformation of Arg385, which is a key residue for GAP activity, was found to be different from that of previously reported GAP proteins, and MgcRacGAP (residues 348-546) was found to exist as a monomer in solution, according to Stokes radii. We also measured the GAP activity of MgcRacGAP mutants for Rac1. PubMed: 23665020 DOI: 10.1016/j.bbrc.2013.04.094 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.9 Å)

Structure validation