1tbg
From Proteopedia
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| - | [[Image:1tbg.jpg|left|200px]] | + | [[Image:1tbg.jpg|left|200px]] |
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| - | '''BETA-GAMMA DIMER OF THE HETEROTRIMERIC G-PROTEIN TRANSDUCIN''' | + | {{Structure |
| + | |PDB= 1tbg |SIZE=350|CAPTION= <scene name='initialview01'>1tbg</scene>, resolution 2.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''BETA-GAMMA DIMER OF THE HETEROTRIMERIC G-PROTEIN TRANSDUCIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TBG is a [ | + | 1TBG is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. The following page contains interesting information on the relation of 1TBG with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb58_1.html G Proteins]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TBG OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8552196 8552196] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: G Proteins]] | [[Category: G Proteins]] | ||
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[[Category: transducer]] | [[Category: transducer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:16:25 2008'' |
Revision as of 12:16, 20 March 2008
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| 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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