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Human
The apo state structure of human Organic Anion Transporter 1 (hOAT1), determined by cryo-EM, reveals the transporter in an inward-facing conformation. This means the central substrate-binding cavity is open toward the intracellular side of the membrane, ready to release a substrate or accept one from the cytoplasm.
OAT1 adopts an inward-facing conformation in a membrane. OAT1 consist of structural features
including intracellular helices domain (ICD),
extracellular domain (ECD), N-lobe helices
(TM1-6), and C-lobe helices (TM7-12). (right) The
border of the binding cavity (described in solvent
exclude-surface) is formed by residues N35,
Y230, Y353, Y354 (upper), and M207 and F442
(lower).


'''Key Structural Characteristics:'''
'''Key Structural Characteristics:'''