1tbg
From Proteopedia
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+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tbg OCA], [http://www.ebi.ac.uk/pdbsum/1tbg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tbg RCSB]</span> | ||
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[[Category: transducer]] | [[Category: transducer]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:53:55 2008'' |
Revision as of 20:53, 30 March 2008
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, resolution 2.1Å | |||||||
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
BETA-GAMMA DIMER OF THE HETEROTRIMERIC G-PROTEIN TRANSDUCIN
Overview
Many signalling cascades use seven-helical transmembrane receptors coupled to heterotrimeric G proteins (G alpha beta gamma) to convert extracellular signals into intracellular responses. Upon nucleotide exchange catalysed by activated receptors, heterotrimers dissociate into GTP-bound G alpha subunits and G beta gamma dimers, either of which can modulate many downstream effectors. Here we use multiwavelength anomalous diffraction data to solve the crystal structure of the beta gamma dimer of the G protein transducin. The beta-subunit is primarily a seven-bladed beta-propeller that is partially encircled by an extended gamma-subunit. The beta-propeller, which contains seven structurally similar WD repeats, defines the stereochemistry of the WD repeat and the probable architecture of all WD-repeat-containing domains. The structure details interactions between G protein beta- and gamma-subunits and highlights regions implicated in effector modulation for the conserved family of G protein beta gamma dimers.
About this Structure
1TBG is a Protein complex structure of sequences from Bos taurus. The following page contains interesting information on the relation of 1TBG with [G Proteins]. Full crystallographic information is available from OCA.
Reference
Crystal structure of a G-protein beta gamma dimer at 2.1A resolution., Sondek J, Bohm A, Lambright DG, Hamm HE, Sigler PB, Nature. 1996 Jan 25;379(6563):369-74. PMID:8552196
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