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The kinetics of the interaction of Rab7 with REP-1 have been investigated using the fluorescence of GDP and GTP analogs at the active site of Rab7. The results show that REP-1 has higher affinity for the GDP bound form of Rab7 (K d =1 nM) than for the GTP bound form (K d =20 nM). Both affinities should still be sufficient for the formation of stable complexes in the cell. The association...
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