Transducin

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(New page: <StructureSection load='1gp2' size='340' side='right' caption='Structure of rat transducin α and βγ subunits complex with GDP (PDB code 1gp2).' scene=''> == Function == '''Trans...)
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<StructureSection load='' size='350' side='right' caption='Structure of rat transducin α (deepskyblue), β (green) and γ (gold) subunits complex with GDP (PDB code [[1gp2]]).' scene='59/590984/Cv/1' pspeed='8'>
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<StructureSection load='1gp2' size='340' side='right' caption='Structure of rat transducin α and βγ subunits complex with GDP (PDB code [[1gp2]]).' scene=''>
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__TOC__
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== Function ==
== Function ==
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'''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.
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'''Transducin''' (TDN) or '''Heterotrimeric G protein''' or '''Guanine nucleotide-binding protein G''' is a <scene name='59/590984/Cv/5'>heterotrimeric G protein containing 3 chains: α, β and γ</scene> 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 <scene name='59/590984/Cv/6'>GDP bound to its α subunit</scene> 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 TDN preventing its re-association with the α subunit.
== Disease ==
== Disease ==
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Congenital stationary night blindness (Nougaret disease) is caused by a mutation in TDN α subunit<ref>PMID:8673138</ref>.
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== Relevance ==
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== Structural highlights ==
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==3D structures of transducin==
==3D structures of transducin==
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[[Transducin 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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'''Transducin-α'''
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[[1tnd]] – bTDN + GTPγS - bovine<br />
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[[1tag]] – bTDN + GDP<br />
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[[3v00]] – b/ratTDN + GDP<br />
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[[1tad]] – bTDN + GDP + AlF4<br />
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[[1fqk]] – bTDN + RGS9 + GDP + AlF4<br />
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[[1fqj]] – bTDN + RGS9 + GMP-PDE γ + GDP + AlF4<br />
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'''Transducin-βγ'''
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[[1tbg]] – bTDN <br />
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[[2trc]], [[1a0r]], [[1b9x]], [[1b9y]] – bTDN + phosducin<br />
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[[1omw]], [[3cik]] – bTDN + G-protein coupled receptor kinase 2<br />
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[[3v5w]] – bTDN (mutant) + G-protein coupled receptor kinase 2<br />
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[[3psc]], [[3pvu]], [[3pvw]], [[4mk0]] – bTDN + β-adrenergic receptor kinase 1<br />
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[[2bcj]] – bTDN (mutant) + β-adrenergic receptor kinase 1<br />
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[[3uzs]] – bTDN + β-adrenergic receptor kinase 1 + RNA<br />
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[[3krw]], [[3krx]] – bTDN + G-protein coupled receptor kinase 2 + inhibitor<br />
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[[1xhm]] – bTDN + peptide<br />
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[[4kfm]] – hTDN + G-protein activated inward rectifier K+ channel<br />
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'''Transducin-α+βγ'''
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[[1got]] – bTDN + GDP<br />
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[[1gg2]] – rTDN + GDP - rat<br />
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[[1gp2]] – rTDN (mutant) + GDP <br />
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[[3ah8]] – bTDN (mutant) + GDP + inhibitor<br />
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[[3sn6]] – bTDN (mutant) + endolysine + antibody fragment<br />
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== References ==
== References ==

Current revision

Structure of rat transducin α (deepskyblue), β (green) and γ (gold) subunits complex with GDP (PDB code 1gp2).

Drag the structure with the mouse to rotate

References

  1. Lerea CL, Bunt-Milam AH, Hurley JB. Alpha transducin is present in blue-, green-, and red-sensitive cone photoreceptors in the human retina. Neuron. 1989 Sep;3(3):367-76. PMID:2534964
  2. Dryja TP, Hahn LB, Reboul T, Arnaud B. Missense mutation in the gene encoding the alpha subunit of rod transducin in the Nougaret form of congenital stationary night blindness. Nat Genet. 1996 Jul;13(3):358-60. PMID:8673138 doi:http://dx.doi.org/10.1038/ng0796-358

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Jaime Prilusky, Joel L. Sussman

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