| Résumé | Adenosine 5'-triphosphate (ATP) binds to a great number of proteins to elicit a wide variety of effects, including energy production and molecular signalling. Proteins have evolved different strategies to specifically recognize ATP, utilizing different ways of binding the phosphoryl moieties as well as the adenine base. The most common, conserved sequence and structural motif for binding ATP is the Walker-A motif, or P-loop, found in many different protein structural families. Greater variation in the sequence of the P-loop is being recognized, as more ATP-binding proteins are being structurally and functionally characterized. In contrast to the P-loop, recognition of the adenine base often makes use of conserved structural motifs of main-chain atoms via hydrogen-bonding interactions, or side-chains in stacking interactions, without a definitive amino acid sequence pattern. |
|---|
