Anterior gradient protein: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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 == Structural highlights ==
 This protein contains various remarkable domains which can be visualized in the figure.
-   -''' an unfolded NH2 terminal sequence with a peptide signal from the first to the 21st amino acid'''
+   '''- an unfolded NH2 terminal sequence with a peptide signal from the first to the 21st amino acid'''
-   - an active pseudo-thioredoxin domain (<scene name='87/872187/Agr2_cxxs/2'>CXXS</scene>) from the 81st to the 84th amino acid. Called “pseudo” because there is only one active cysteine residue (C81)
+   '''- an active pseudo-thioredoxin domain (<scene name='87/872187/Agr2_cxxs/2'>CXXS</scene>) from the 81st to the 84th amino acid. Called “pseudo” because there is only one active cysteine residue (C81)
-   - a terminal COOH sequence with a KTEL motif from the 172nd to the last
+   - a terminal COOH sequence with a KTEL motif from the 172nd to the last'''
 Moreover, this protein can be found as a monomer or a dimer, thanks to a specific motif which is EALYK between the 60th and the 64th amino acids. There are intermolecular salt bridges involving E60 and K64, in order to fix the second monomer. The CXXS domain is on the opposite side to avoid any disulfide exchange. Nevertheless, the dimeric structure is oxidation-dependent which means that C81 is necessary.