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- W2005851263 abstract "Gelsolin is built up of six homologous segments that perform different functions on actin. Segments 1 and 2, which are suggested to be highly similar in their overall folds, bind monomeric and filamentous actin respectively. A long α‐helix in segment 1 forms the major contact site of this segment with actin. We show that sequence 197–226 of segment 2, equivalent to the region around the actin binding helix in segment 1, contains F‐actin binding activity. Consequently, positionally similar parts of segment 1 and 2 are implicated in the actin contact and solvent exposed residues in these parts must have evolved differentially to meet their different actin binding properties." @default.
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- W2005851263 date "1996-11-18" @default.
- W2005851263 modified "2023-10-14" @default.
- W2005851263 title "Evidence for an actin binding helix in gelsolin segment 2; have homologous sequences in segments 1 and 2 of gelsolin evolved to divergent actin binding functions?" @default.
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- W2005851263 doi "https://doi.org/10.1016/s0014-5793(96)01086-1" @default.
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