6YJK
Structure of CYRI-B (FAM49B) from Rhincodon typus
Summary for 6YJK
| Entry DOI | 10.2210/pdb6yjk/pdb |
| Related | 6YJJ |
| Descriptor | CYRI-B (FAM49B) (2 entities in total) |
| Functional Keywords | cyri-b, fam49b, actin assembly, rac binding protein, cell motility regulator, cytosolic protein |
| Biological source | Rhincodon typus (Whale shark) |
| Total number of polymer chains | 1 |
| Total formula weight | 36909.91 |
| Authors | Kaplan, E. (deposition date: 2020-04-03, release date: 2020-10-14, Last modification date: 2024-01-24) |
| Primary citation | Kaplan, E.,Stone, R.,Hume, P.J.,Greene, N.P.,Koronakis, V. Structure of CYRI-B (FAM49B), a key regulator of cellular actin assembly. Acta Crystallogr D Struct Biol, 76:1015-1024, 2020 Cited by PubMed Abstract: In eukaryotes, numerous fundamental processes are controlled by the WAVE regulatory complex (WRC) that regulates cellular actin polymerization, crucial for cell motility, cell-cell adhesion and epithelial differentiation. Actin assembly is triggered by interaction of the small GTPase Rac1 with CYFIP1, a key component of the WRC. Previously known as FAM49B, CYRI-B is a protein that is highly conserved across the Eukaryota and has recently been revealed to be a key regulator of Rac1 activity. Mutation of CYRI-B or alteration of its expression therefore leads to altered actin nucleation dynamics, with impacts on lamellipodia formation, cell migration and infection by intracellular pathogens. In addition, knockdown of CYRI-B expression in cancer cell lines results in accelerated cell proliferation and invasiveness. Here, the structure of Rhincodon typus (whale shark) CYRI-B is presented, which is the first to be reported of any CYRI family member. Solved by X-ray crystallography, the structure reveals that CYRI-B comprises three distinct α-helical subdomains and is highly structurally related to a conserved domain present in CYFIP proteins. The work presented here establishes a template towards a better understanding of CYRI-B biological function. PubMed: 33021503DOI: 10.1107/S2059798320010906 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.37 Å) |
Structure validation
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