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Fig. 1 | Human Genomics

Fig. 1

From: The complex impact of cancer-related missense mutations on the stability and on the biophysical and biochemical properties of MAPK1 and MAPK3 somatic variants

Fig. 1

Sequence alignment, structure and variants of MAPK1 and MAPK3. a Secondary structure elements (alpha helices in red rectangles, beta-sheet in cyan arrows) are shown at the top (MAPK1) and at the bottom (MAPK3) of the sequence alignment. Mutated residues in MAPK1 and MAPK3 variants are highlighted in red. F-site residues are shown in bold. Pink box: Gly-rich loop; red box: αC-helix; blue box: hinge region; green box: activation loop; CD-site: cyan box. Asterisks indicate the fully conserved residues. b Superposition of human MAPK1 (in magenta, pdb: 1TVO), and MAPK3 wild type (secondary structure color, pdb: 4QTB). The residues T185 and Y187 (MAPK1), and T202 and Y204 (MAPK3) important for the protein activation are represented in ball and stick. c MAPK1 and MAPK3 variants object of these studies

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Human Genomics

ISSN: 1479-7364