1tag

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(New page: 200px<br /><applet load="1tag" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tag, resolution 1.8&Aring;" /> '''STRUCTURAL DETERMINAN...)
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[[Image:1tag.gif|left|200px]]<br /><applet load="1tag" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1tag.gif|left|200px]]<br /><applet load="1tag" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1tag, resolution 1.8&Aring;" />
caption="1tag, resolution 1.8&Aring;" />
'''STRUCTURAL DETERMINANTS FOR ACTIVATION OF THE ALPHA-SUBUNIT OF A HETEROTRIMERIC G PROTEIN'''<br />
'''STRUCTURAL DETERMINANTS FOR ACTIVATION OF THE ALPHA-SUBUNIT OF A HETEROTRIMERIC G PROTEIN'''<br />
==Overview==
==Overview==
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The 1.8 A crystal structure of transducin alpha.GDP, when compared to that, of the activated complex with GTP-gamma S, reveals the nature of the, conformational changes that occur on activation of a heterotrimeric, G-protein alpha-subunit. Structural changes initiated by direct contacts, with the terminal phosphate of GTP propagate to regions that have been, implicated in effector activation. The changes are distinct from those, observed in other members of the GTPase superfamily.
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The 1.8 A crystal structure of transducin alpha.GDP, when compared to that of the activated complex with GTP-gamma S, reveals the nature of the conformational changes that occur on activation of a heterotrimeric G-protein alpha-subunit. Structural changes initiated by direct contacts with the terminal phosphate of GTP propagate to regions that have been implicated in effector activation. The changes are distinct from those observed in other members of the GTPase superfamily.
==About this Structure==
==About this Structure==
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1TAG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with MG and GDP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TAG OCA].
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1TAG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TAG OCA].
==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Hamm, H.E.]]
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[[Category: Hamm, H E.]]
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[[Category: Lambright, D.G.]]
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[[Category: Lambright, D G.]]
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[[Category: Noel, J.P.]]
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[[Category: Noel, J P.]]
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[[Category: Sigler, P.B.]]
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[[Category: Sigler, P B.]]
[[Category: GDP]]
[[Category: GDP]]
[[Category: MG]]
[[Category: MG]]
[[Category: gtp-binding protein]]
[[Category: gtp-binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:07:05 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:11:34 2008''

Revision as of 13:11, 21 February 2008


1tag, resolution 1.8Å

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STRUCTURAL DETERMINANTS FOR ACTIVATION OF THE ALPHA-SUBUNIT OF A HETEROTRIMERIC G PROTEIN

Overview

The 1.8 A crystal structure of transducin alpha.GDP, when compared to that of the activated complex with GTP-gamma S, reveals the nature of the conformational changes that occur on activation of a heterotrimeric G-protein alpha-subunit. Structural changes initiated by direct contacts with the terminal phosphate of GTP propagate to regions that have been implicated in effector activation. The changes are distinct from those observed in other members of the GTPase superfamily.

About this Structure

1TAG is a Single protein structure of sequence from Bos taurus with and as ligands. Full crystallographic information is available from OCA.

Reference

Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein., Lambright DG, Noel JP, Hamm HE, Sigler PB, Nature. 1994 Jun 23;369(6482):621-8. PMID:8208289

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