Structure of Shroom domain 2 reveals a three-segmented coiled-coil required for dimerization, Rock binding, and apical constriction

By S. Mohan, Ryan Rizaldy, Debamitra Das, R. Bauer, A. Héroux, M. Trakselis, J. Hildebrand, Andrew P. Vandemark. 2012

41 citations recorded by the source corpus.

The Shrm SD2 region contains a core that adopts a novel three-segmented dimer required for Rock binding. Conserved interfaces critical for Rock binding, ppMLC levels, and the formation of contractile cytoskeletal networks are identified. The complex is likely tetrameric, which suggests that conformational changes within SD2 are likely upon Rock binding.

Subfields: Cell Biology, Cellular and Molecular Neuroscience, Molecular Biology

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In Cellular and Molecular Neuroscience

1. Jinbo Xu
2. Sheng Wang

In Molecular Biology

1. Sheng Wang
2. Jinbo Xu
3. Siqi Sun
4. Z. Li
5. Renyu Zhang
6. Badri Adhikari
7. David T. Jones
8. Jianlin Cheng

Citations in the corpus

• Accurate De Novo Prediction of Protein Contact Map by Ultra-Deep Learning Model (2016, background): “In particular, 3thfA is a dimer and each monomer adopts a fold consisting of three segmented anti-parallel coiled-coil[42], whereas 5f5pH is a monomer that adopts a two segmented antiparallel coiled-coil[41] Superimposing the Human SD2 monomer onto the Drosophila SD2 dimer shows that the former stru”
• Structure of the Shroom-Rho Kinase Complex Reveals a Binding Interface with Monomeric Shroom That Regulates Cell Morphology and Stimulates Kinase Activity* (2016, methodology): “Surprisingly, the structure of the SD2 domain from Drosophila Shrm revealed that this conserved domain adopted a three-segmented, antiparallel coiled coil with mutational analysis indicating two Rock-binding sites located 80 Å apart (44).”