Transducin: Difference between revisions
Jump to navigation
Jump to search
Michal Harel (talk | contribs) No edit summary |
Michal Harel (talk | contribs) No edit summary |
||
Line 4: | Line 4: | ||
== Function == | == Function == | ||
'''Transducin''' (TDN) is a heterotrimeric G protein containing 3 chains: α, β and γ which are organized in two subunits: α and βγ. TDN is involved in phototransduction. The absorption of a photon by retinal causes a change in the conformation of rhodopsin into metarhodopsin II. The latter causes activation of TDN. Upon TDN activation the GDP bound to its α subunit is exchanged for the GTP from the cytoplasm. Deactivation of TDN occurs when the GTP bound to the α subunit is hydrolyzed to GDP. Phosducin binds to the βγ subunit of TND preventing its reassociation with the α subunit. | '''Transducin''' (TDN) is a heterotrimeric G protein containing 3 chains: α, β and γ which are organized in two subunits: α and βγ<ref>PMID:2534964</ref>. TDN is involved in phototransduction. The absorption of a photon by retinal causes a change in the conformation of rhodopsin into metarhodopsin II. The latter causes activation of TDN. Upon TDN activation the GDP bound to its α subunit is exchanged for the GTP from the cytoplasm. Deactivation of TDN occurs when the GTP bound to the α subunit is hydrolyzed to GDP. Phosducin binds to the βγ subunit of TND preventing its reassociation with the α subunit. | ||
== Disease == | == Disease == |
Revision as of 13:41, 20 September 2016
FunctionTransducin (TDN) is a heterotrimeric G protein containing 3 chains: α, β and γ which are organized in two subunits: α and βγ[1]. TDN is involved in phototransduction. The absorption of a photon by retinal causes a change in the conformation of rhodopsin into metarhodopsin II. The latter causes activation of TDN. Upon TDN activation the GDP bound to its α subunit is exchanged for the GTP from the cytoplasm. Deactivation of TDN occurs when the GTP bound to the α subunit is hydrolyzed to GDP. Phosducin binds to the βγ subunit of TND preventing its reassociation with the α subunit. DiseaseRelevanceStructural highlights |
|
3D structures of transducin3D structures of transducin
Updated on 20-September-2016