Extended Data Fig. 6: Conservation of SPIN90 residues involved in dimerization and interactions with Arp2/3 complex. | Nature Structural & Molecular Biology

Extended Data Fig. 6: Conservation of SPIN90 residues involved in dimerization and interactions with Arp2/3 complex.

From: Activation of Arp2/3 complex by a SPIN90 dimer in linear actin-filament nucleation

Extended Data Fig. 6

a, Highly conserved residues of SPIN90 shown in purple belong to regions (1) involved in dimerization of SPIN90 (MSDR) in MS, (2) interaction with Arp3, and (3) clamp binding via the leucine rich domain (LRD) based on ConSurf analysis. b, Multiple sequence alignment of human SPIN90 with ten other metazoan species. Residues that interact with Arp2/3 complex and show sequence identity across metazoans have been highlighted. Details of sequences and alignments have been described in the methods.

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