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WAAR WIJ TROTS OP ZIJN

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Entropy of Class-A GPCRs<br />

3<br />

2<br />

1<br />

0<br />

0<br />

3.32<br />

6.37<br />

5.48<br />

3.25<br />

3.50<br />

3.43<br />

5.35<br />

4.47<br />

Binding site<br />

Conserved<br />

Extracellular end of helices<br />

Helix-helix interaction<br />

Facing membrane<br />

Mixed region<br />

20 40 60<br />

Sum of subfamilies’ entropies<br />

Clustering positions in the two-entropies plot into different<br />

functional categories. The magenta dots ◆, for instance, refer<br />

to individual amino acids that are highly conserved, probably<br />

playing a role in the activation mechanism of the receptors.<br />

Numbers refer to specific amino acid positions in the receptors,<br />

such as red-dotted 3.32 ● in the third trans-membrane domain,<br />

which supposedly plays an important role in drug binding.<br />

The red dots ● in the two-entropies plot correspond to the red<br />

amino acids ✕ in the receptor structure. They are lining the<br />

(yellow) ligand-binding site.<br />

39

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