Membrane proteins account for roughly 30 percent of all open reading frames in fully sequenced genomes. However, to date, atomic structures have so far been obtained for only 424 integral membrane proteins, with 100 new structures determined in the last two years. Only 10 percent of the unique integral membrane protein structures are derived from vertebrates. In general, integral membrane proteins are present in tissues at very low concentration, making production of recombinant proteins in heterologous systems suitable for large scale production a prerequisite for structural studies. Since the first atomic structures of recombinant mammalian integral membrane proteins published in 2005 (the calcium ATPase SERCA 1A and a voltage-dependent potatium channel), the structures of 37 recombinant mammalian integral membrane proteins, from which 20 belong to the G Protein Coupled Receptors family, have been solved.
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