INVESTIGADORES
BOUZAT Cecilia Beatriz
artículos
Título:
Structural Basis of Activation of Cys-Loop Receptors: the ExtracellularTransmembrane Interface as a Coupling Region
Autor/es:
M BARTOS,; J CORRADI; C BOUZAT
Revista:
MOLECULAR NEUROBIOLOGY
Editorial:
HUMANA PRESS INC
Referencias:
Año: 2009 vol. 40 p. 236 - 252
ISSN:
0893-7648
Resumen:
Cys-loop receptors mediate rapid transmission
throughout the nervous system by converting a chemical
signal into an electric one. They are pentameric proteins
with an extracellular domain that carries the transmitter
binding sites and a transmembrane region that forms the ion
pore. Their essential function is to couple the binding of the
agonist at the extracellular domain to the opening of the ion
pore. How the structural changes elicited by agonist
binding are propagated through a distance of 50Å to the
gate is therefore central for the understanding of the
receptor function. A step forward toward the identification
of the structures involved in gating has been given by the
recently elucidated high-resolution structures of Cys-loop
receptors and related proteins. The extracellulartransmembrane
interface has attracted attention because it is a
structural transition zone where β-sheets from the extracellular
domain merge with α-helices from the transmembrane
domain. Within this zone, several regions form a network
that relays structural changes from the binding site toward
the pore, and therefore, this interface controls the beginning
and duration of a synaptic response. In this review, the most
recent findings on residues and pairwise interactions
underlying channel gating are discussed, the main focus
being on the extracellulartransmembrane interface.transmembrane
interface has attracted attention because it is a
structural transition zone where β-sheets from the extracellular
domain merge with α-helices from the transmembrane
domain. Within this zone, several regions form a network
that relays structural changes from the binding site toward
the pore, and therefore, this interface controls the beginning
and duration of a synaptic response. In this review, the most
recent findings on residues and pairwise interactions
underlying channel gating are discussed, the main focus
being on the extracellulartransmembrane interface.β-sheets from the extracellular
domain merge with α-helices from the transmembrane
domain. Within this zone, several regions form a network
that relays structural changes from the binding site toward
the pore, and therefore, this interface controls the beginning
and duration of a synaptic response. In this review, the most
recent findings on residues and pairwise interactions
underlying channel gating are discussed, the main focus
being on the extracellulartransmembrane interface.α-helices from the transmembrane
domain. Within this zone, several regions form a network
that relays structural changes from the binding site toward
the pore, and therefore, this interface controls the beginning
and duration of a synaptic response. In this review, the most
recent findings on residues and pairwise interactions
underlying channel gating are discussed, the main focus
being on the extracellulartransmembrane interface.transmembrane interface.