1got

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(New page: 200px<br /> <applet load="1got" size="450" color="white" frame="true" align="right" spinBox="true" caption="1got, resolution 2.0&Aring;" /> '''HETEROTRIMERIC COMPL...)
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[[Image:1got.gif|left|200px]]<br />
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[[Image:1got.gif|left|200px]]<br /><applet load="1got" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1got" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1got, resolution 2.0&Aring;" />
caption="1got, resolution 2.0&Aring;" />
'''HETEROTRIMERIC COMPLEX OF A GT-ALPHA/GI-ALPHA CHIMERA AND THE GT-BETA-GAMMA SUBUNITS'''<br />
'''HETEROTRIMERIC COMPLEX OF A GT-ALPHA/GI-ALPHA CHIMERA AND THE GT-BETA-GAMMA SUBUNITS'''<br />
==Overview==
==Overview==
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The structure of a heterotrimeric G protein reveals the mechanism of the, nucleotide-dependent engagement of the alpha and beta gamma subunits that, regulates their interaction with receptor and effector molecules. The, interaction involves two distinct interfaces and dramatically alters the, conformation of the alpha but not of the beta gamma subunits. The location, of the known sites for post-translational modification and receptor, coupling suggest a plausible orientation with respect to the membrane, surface and an activated heptahelical receptor.
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The structure of a heterotrimeric G protein reveals the mechanism of the nucleotide-dependent engagement of the alpha and beta gamma subunits that regulates their interaction with receptor and effector molecules. The interaction involves two distinct interfaces and dramatically alters the conformation of the alpha but not of the beta gamma subunits. The location of the known sites for post-translational modification and receptor coupling suggest a plausible orientation with respect to the membrane surface and an activated heptahelical receptor.
==About this Structure==
==About this Structure==
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1GOT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with GDP as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1GOT 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GOT OCA].
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1GOT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1GOT 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=1GOT OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Bohm, A.]]
[[Category: Bohm, A.]]
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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: Sigler, P.B.]]
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[[Category: Sigler, P B.]]
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[[Category: Skiba, N.P.]]
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[[Category: Skiba, N P.]]
[[Category: Sondek, J.]]
[[Category: Sondek, J.]]
[[Category: GDP]]
[[Category: GDP]]
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[[Category: heterotrimer signal transduction]]
[[Category: heterotrimer signal transduction]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:00:56 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:52:21 2008''

Revision as of 10:52, 21 February 2008


1got, resolution 2.0Å

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HETEROTRIMERIC COMPLEX OF A GT-ALPHA/GI-ALPHA CHIMERA AND THE GT-BETA-GAMMA SUBUNITS

Overview

The structure of a heterotrimeric G protein reveals the mechanism of the nucleotide-dependent engagement of the alpha and beta gamma subunits that regulates their interaction with receptor and effector molecules. The interaction involves two distinct interfaces and dramatically alters the conformation of the alpha but not of the beta gamma subunits. The location of the known sites for post-translational modification and receptor coupling suggest a plausible orientation with respect to the membrane surface and an activated heptahelical receptor.

About this Structure

1GOT is a Protein complex structure of sequences from Bos taurus with as ligand. The following page contains interesting information on the relation of 1GOT with [G Proteins]. Full crystallographic information is available from OCA.

Reference

The 2.0 A crystal structure of a heterotrimeric G protein., Lambright DG, Sondek J, Bohm A, Skiba NP, Hamm HE, Sigler PB, Nature. 1996 Jan 25;379(6563):311-9. PMID:8552184

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