Summary for 7AJL
| Entry DOI | 10.2210/pdb7ajl/pdb |
| Descriptor | CYFIP-related Rac1 interactor B (2 entities in total) |
| Functional Keywords | rac1 competitor, actin regulation, scar/wave inhibitor, cytosolic protein |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 2 |
| Total formula weight | 68799.49 |
| Authors | Yelland, T.,Anh, H.,Insall, R.,Machesky, L.,Ismail, S. (deposition date: 2020-09-29, release date: 2020-11-18, Last modification date: 2024-10-16) |
| Primary citation | Yelland, T.,Le, A.H.,Nikolaou, S.,Insall, R.,Machesky, L.,Ismail, S. Structural Basis of CYRI-B Direct Competition with Scar/WAVE Complex for Rac1. Structure, 29:226-237.e4, 2021 Cited by PubMed Abstract: Rac1 is a major regulator of actin dynamics, with GTP-bound Rac1 promoting actin assembly via the Scar/WAVE complex. CYRI competes with Scar/WAVE for interaction with Rac1 in a feedback loop regulating actin dynamics. Here, we reveal the nature of the CYRI-Rac1 interaction, through crystal structures of CYRI-B lacking the N-terminal helix (CYRI-BΔN) and the CYRI-BΔN:Rac1Q61L complex, providing the molecular basis for CYRI-B regulation of the Scar/WAVE complex. We reveal CYRI-B as having two subdomains - an N-terminal Rac1 binding subdomain with a unique Rac1-effector interface and a C-terminal Ratchet subdomain that undergoes conformational changes induced by Rac1 binding. Finally, we show that the CYRI protein family, CYRI-A and CYRI-B can produce an autoinhibited hetero- or homodimers, adding an additional layer of regulation to Rac1 signaling. PubMed: 33217330DOI: 10.1016/j.str.2020.11.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.37 Å) |
Structure validation
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