1tbg: Difference between revisions

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==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.

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==

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[[Category: Protein complex]]

[[Category: Bohm, A.]]

[[Category: Hamm, H.E.]]

[[Category: Hamm, H E.]]

[[Category: Lambright, D.G.]]

[[Category: Lambright, D G.]]

[[Category: Sigler, P.B.]]

[[Category: Sigler, P B.]]

[[Category: Sondek, J.S.]]

[[Category: Sondek, J S.]]

[[Category: complex (gtp-binding/transducer)]]

[[Category: eye]]

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[[Category: transducer]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 15: / Line 15: @@
 [[Category: Protein complex]]
 [[Category: Bohm, A.]]
-[[Category: Hamm, H.E.]]
+[[Category: Hamm, H E.]]
-[[Category: Lambright, D.G.]]
+[[Category: Lambright, D G.]]
-[[Category: Sigler, P.B.]]
+[[Category: Sigler, P B.]]
-[[Category: Sondek, J.S.]]
+[[Category: Sondek, J S.]]
 [[Category: complex (gtp-binding/transducer)]]
 [[Category: eye]]
@@ Line 24: / Line 24: @@
 [[Category: transducer]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:56:10 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:11:49 2008''