Key result
WH2 domains bind actin with approximately 10-fold higher affinity than the Tbeta domain, inhibiting nucleotide exchange by targeting the cleft between actin subdomains 1 and 3.
Population
Actin complexes with the WH2 domains of WASP, WASP-family verprolin homologous protein, and WASP-interacting…
Comparison
Crystal structure analysis vs Thymosin beta domain (Tbeta)
Design
Preclinical
Authors
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Advances molecular models of actin regulation; leaves open validation for cytoskeletal disease therapies.
Crystal structures of actin-WH2 complexes reveal the structural basis for actin binding and suggest mechanisms for filament nucleation and elongation by WASP-family proteins.
Chéreau et al. (2005) studied this question. WH2 domains vs. Tbeta domain was evaluated on Actin binding affinity and structural characteristics. WH2 domains bind actin with approximately 10-fold higher affinity than the Tbeta domain, inhibiting nucleotide exchange by targeting the cleft between actin subdomains 1 and 3.
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