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7AJK

Crystal structure of CRYI-B Rac1 complex

This is a non-PDB format compatible entry.
Summary for 7AJK
Entry DOI10.2210/pdb7ajk/pdb
DescriptorRas-related C3 botulinum toxin substrate 1, CYFIP-related Rac1 interactor B, MAGNESIUM ION, ... (5 entities in total)
Functional Keywordsactin, cytoskeleton, rac1, gtpase, inhibitor, cytosolic protein
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains2
Total formula weight57232.29
Authors
Yelland, T.,Anh, L.,Insall, R.,Machesky, L.,Ismail, S. (deposition date: 2020-09-29, release date: 2020-11-18, Last modification date: 2024-01-31)
Primary citationYelland, 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: 33217330
DOI: 10.1016/j.str.2020.11.003
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

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数据于2025-06-11公开中

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