1got
From Proteopedia
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[[Image:1got.gif|left|200px]] | [[Image:1got.gif|left|200px]] | ||
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'''HETEROTRIMERIC COMPLEX OF A GT-ALPHA/GI-ALPHA CHIMERA AND THE GT-BETA-GAMMA SUBUNITS''' | '''HETEROTRIMERIC COMPLEX OF A GT-ALPHA/GI-ALPHA CHIMERA AND THE GT-BETA-GAMMA SUBUNITS''' | ||
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[[Category: Skiba, N P.]] | [[Category: Skiba, N P.]] | ||
[[Category: Sondek, J.]] | [[Category: Sondek, J.]] | ||
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| - | + | [[Category: Heterotrimer signal transduction]] | |
| - | [[Category: | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:50:03 2008'' |
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Revision as of 14:50, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 17:50:03 2008
