Key result
Profilin I mutations W3N and H133S abolished poly(L-proline)-binding activity and reduced affinity for actin, indicating the poly(L-proline)-binding surface is a crucial regulatory site.
The poly(L-proline)-binding surface of profilin is a crucial regulatory site that affects the distantly located actin-binding site.
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Hypothesis-generating for profilin regulation in actin dynamics; leaves open validation in cardiac disease models.
Sjögren et al. (1997) studied this question. Profilin I mutants (W3N and H133S) vs. Wild-type profilin was evaluated on Binding to poly(L-proline), actin, and PIP2. Profilin I mutations W3N and H133S abolished poly(L-proline)-binding activity and reduced affinity for actin, indicating the poly(L-proline)-binding surface is a crucial regulatory site.
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