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Fig. 1 | Molecular Medicine

Fig. 1

From: Lasp-1, a Novel Type of Actin-Binding Protein Accumulating in Cell Membrane Extensions

Fig. 1

Lasp-1 protein organization. (A) Schematic representation of human Lasp-1 (261 amino acids). The LIM domain, actin-binding repeats (R1 and R2), and SH3 domain are dotted, hatched, and gray, respectively. Alignment of the LIM (B), actin-binding (C), and SH3 (D) domains of Lasp-1 with corresponding domains of N-Rap, nebulin, nebulette, and Ylz4. h, human; m, mouse; c, chicken; ce, Caenorhabditis elegans. Amino acids are designated by the one-letter code, and numbers indicate their position. Gaps (.) are introduced to optimize the alignment.

Residues conserved in all (B, D) or in four out of five (C) sequences are in boldface and reported in the consensus sequence. In (B), cysteines and histidines involved in the LIM domain are shown by closed circles. In (C), only the repeats of nebulin, N-Rap, and nebulette that are the most homologous with those of Lasp-1 are represented. The conserved SD—YK motifs of nebulin-like actin-binding repeats are marked by open circles. In (D), the asterisks indicate the last residue of the proteins.

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