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. 2001 Mar 13;98(6):3115–3120. doi: 10.1073/pnas.051631098

Figure 1.

Figure 1

(Upper) Summary of domain mapping within human RAP74 by using limited proteolysis combined with mass spectrometry. Arrows indicate cleavage sites observed within minutes to hours. (Lower) Sequence alignments of the C-terminal regions of RAP74 from human (H.sap), Xenopus laevis, Drosophila melanogaster, Caenorhabditis elegans, and Saccharomyces cerevisiae. Secondary structure elements observed in the hRAP74cc crystal structure are also shown. Structure-based sequence alignments of the C-terminal domain of human RAP30, the middle domain of TFIIEβ, and the DNA-binding domains of HNF-3γ and RFX1 are given below. Red letters denote DNA-binding residues identified by x-ray crystallography or NMR. Magenta and yellow letters denote putative FCP1-binding regions identified in yeast and residues constituting the hydrophobic concave surface of hRAP74cc, respectively.