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. 2005 Sep 19;102(39):13891–13896. doi: 10.1073/pnas.0502390102

Fig. 4.

Fig. 4.

The ccCor1 sequence Arg-450–Glu-455 is conserved in intracellular (I), extracellular (II), transmembrane (III), viral (IV), and synthetic (V) proteins containing short three-stranded parallel coiled-coil domains. Sequence alignments of mouse coronin 1A (mCor-1A) with the coiled-coil domains of human heat shock factor-binding protein 1 (hHSBP1), chicken tenascin C (chTN-C), human matrilin-1 (hMat-1), human type XVII collagen a1 (hXVII), influenza hemagglutinin (HA2), HIV-1 envelope glycoprotein (HIVgp41), and the synthetic ccβ-p coiled coil are shown. Heptad repeats are shown in blocks of seven amino acids, and residues at positions a and d are underlined. The conserved residues forming the trimerization motif in ccCor1 (Fig. 2) are shown in bold and colored according to their physicochemical properties: blue, positively charged; red, negatively charged; green, hydrophobic. The deduced consensus sequence is shown at the bottom. For a full alignment, see Fig. 7.