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. 1999 Apr 19;189(8):1243–1253. doi: 10.1084/jem.189.8.1243

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Structural organization of GrpL and amino acid homology comparison with other Grb2-like proteins. A schematic for the domain organization of GrpL is depicted in the upper part of A. Numbers on top mark amino acid residues at the boundaries of the different domains. The lower part of A shows the amino acid sequence comparison between mouse and human GrpL and B shows the amino acid sequence comparison among mGrpL, hGrpL, Grb2, and Grap. Boxed residues represent homologous regions. Amino acids in bold and shade denote identical residues, while unshaded amino acids denote conserved substitutions. The nucleotide sequences for hGrpL and mGrpL are available from EMBL/ GenBank/DDBJ under accession numbers AF129476 and AF129477.

Structural organization of GrpL and amino acid homology comparison with other Grb2-like proteins. A schematic for the domain organization of GrpL is depicted in the upper part of A. Numbers on top mark amino acid residues at the boundaries of the different domains. The lower part of A shows the amino acid sequence comparison between mouse and human GrpL and B shows the amino acid sequence comparison among mGrpL, hGrpL, Grb2, and Grap. Boxed residues represent homologous regions. Amino acids in bold and shade denote identical residues, while unshaded amino acids denote conserved substitutions. The nucleotide sequences for hGrpL and mGrpL are available from EMBL/ GenBank/DDBJ under accession numbers AF129476 and AF129477.