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All told, given that a common motif is found in many different fold types, it is possible that similar adenine binding sites in these folds arose independently on different occasions rather than from a more prosaic divergent mechanism. The common adenine-binding motif shown in this study is simple to construct. It uses only (1) backbone polar interactions that are not dependent on the protein sequence or particular properties of amino acid sidechains, and (2) nonspecific hydrophobic interactions. This is probably why so many different proteins with different functions use this motif to bind an adenylate-containing ligand. The motif common to many proteins and described in this study is not, however, the only way in which proteins bind adenine-containing ligands. Thus, although a wide variety of different folds bind adenine ligands in a similar way, many other proteins use alternative motifs. Nevertheless, the adenylate-binding motif reported in this article is present in “ancient proteins” common to all living organisms, suggesting that adenine-containing ligands and the common motif for binding them were exploited very early in evolution. The geometry of adenine binding by this motif mimics almost exactly the geometry of adenine base-pairing seen in DNA and RNA.

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se il principio generale dovrebbe essere quello del risparmio e del "riciclaggio"?

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Magari nashita ti saprebbe dare qualche informazione in più, dato che è uno dei suoi campi preferiti

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