5F4Y
Structure of the SD2 domain of Human Shroom2
Summary for 5F4Y
| Entry DOI | 10.2210/pdb5f4y/pdb |
| Related | 3THF |
| Descriptor | Protein Shroom2 (1 entity in total) |
| Functional Keywords | coiled-coil, rock-binding, protein binding |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 42107.91 |
| Authors | Mo, J.H.,Zalewski, J.K.,Heroux, A.,VanDemark, A.P. (deposition date: 2015-12-03, release date: 2016-10-19, Last modification date: 2024-10-30) |
| Primary citation | Zalewski, J.K.,Mo, J.H.,Heber, S.,Heroux, A.,Gardner, R.G.,Hildebrand, J.D.,VanDemark, A.P. Structure of the Shroom-Rho Kinase Complex Reveals a Binding Interface with Monomeric Shroom That Regulates Cell Morphology and Stimulates Kinase Activity. J. Biol. Chem., 291:25364-25374, 2016 Cited by PubMed Abstract: Shroom-mediated remodeling of the actomyosin cytoskeleton is a critical driver of cellular shape and tissue morphology that underlies the development of many tissues including the neural tube, eye, intestines, and vasculature. Shroom uses a conserved SD2 domain to direct the subcellular localization of Rho-associated kinase (Rock), which in turn drives changes in the cytoskeleton and cellular morphology through its ability to phosphorylate and activate non-muscle myosin II. Here, we present the structure of the human Shroom-Rock binding module, revealing an unexpected stoichiometry for Shroom in which two Shroom SD2 domains bind independent surfaces on Rock. Mutation of interfacial residues impaired Shroom-Rock binding in vitro and resulted in altered remodeling of the cytoskeleton and loss of Shroom-mediated changes in cellular morphology. Additionally, we provide the first direct evidence that Shroom can function as a Rock activator. These data provide molecular insight into the Shroom-Rock interface and demonstrate that Shroom directly participates in regulating cytoskeletal dynamics, adding to its known role in Rock localization. PubMed: 27758857DOI: 10.1074/jbc.M116.738559 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.293 Å) |
Structure validation
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