1gdd: Difference between revisions

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New page: left|200px<br /><applet load="1gdd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gdd, resolution 2.2Å" /> '''TERTIARY AND QUATERNA...
 
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[[Image:1gdd.jpg|left|200px]]<br /><applet load="1gdd" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1gdd.jpg|left|200px]]<br /><applet load="1gdd" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1gdd, resolution 2.2&Aring;" />
caption="1gdd, resolution 2.2&Aring;" />
'''TERTIARY AND QUATERNARY STRUCTURAL CHANGES IN GIA1 INDUCED BY GTP HYDROLYSIS'''<br />
'''TERTIARY AND QUATERNARY STRUCTURAL CHANGES IN GIA1 INDUCED BY GTP HYDROLYSIS'''<br />


==Overview==
==Overview==
Crystallographic analysis of 2.2 angstrom resolution shows that guanosine, triphosphate (GTP) hydrolysis triggers conformational changes in the, heterotrimeric G-protein alpha subunit, Gi alpha 1. The switch II and, switch III segments become disordered, and linker II connecting the Ras, and alpha helical domains moves, thus altering the structures of potential, effector and beta gamma binding regions. Contacts between the, alpha-helical and Ras domains are weakened, possibly facilitating the, release of guanosine diphosphate (GDP). The amino and carboxyl termini, which contain receptor and beta gamma binding determinants, are disordered, in the complex with GTP, but are organized into a compact microdomain on, GDP hydrolysis. The amino terminus also forms extensive quaternary, contacts with neighboring alpha subunits in the lattice, suggesting that, multimers of alpha subunits or heterotrimers may play a role in signal, transduction.
Crystallographic analysis of 2.2 angstrom resolution shows that guanosine triphosphate (GTP) hydrolysis triggers conformational changes in the heterotrimeric G-protein alpha subunit, Gi alpha 1. The switch II and switch III segments become disordered, and linker II connecting the Ras and alpha helical domains moves, thus altering the structures of potential effector and beta gamma binding regions. Contacts between the alpha-helical and Ras domains are weakened, possibly facilitating the release of guanosine diphosphate (GDP). The amino and carboxyl termini, which contain receptor and beta gamma binding determinants, are disordered in the complex with GTP, but are organized into a compact microdomain on GDP hydrolysis. The amino terminus also forms extensive quaternary contacts with neighboring alpha subunits in the lattice, suggesting that multimers of alpha subunits or heterotrimers may play a role in signal transduction.


==About this Structure==
==About this Structure==
1GDD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with SO4 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=1GDD OCA].  
1GDD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=SO4:'>SO4</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=1GDD OCA].  


==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Mixon, M.B.]]
[[Category: Mixon, M B.]]
[[Category: Sprang, S.R.]]
[[Category: Sprang, S R.]]
[[Category: GDP]]
[[Category: GDP]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: gtp-ase]]
[[Category: gtp-ase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:57:45 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:53 2008''

Revision as of 13:48, 21 February 2008

File:1gdd.jpg


1gdd, resolution 2.2Å

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TERTIARY AND QUATERNARY STRUCTURAL CHANGES IN GIA1 INDUCED BY GTP HYDROLYSIS

OverviewOverview

Crystallographic analysis of 2.2 angstrom resolution shows that guanosine triphosphate (GTP) hydrolysis triggers conformational changes in the heterotrimeric G-protein alpha subunit, Gi alpha 1. The switch II and switch III segments become disordered, and linker II connecting the Ras and alpha helical domains moves, thus altering the structures of potential effector and beta gamma binding regions. Contacts between the alpha-helical and Ras domains are weakened, possibly facilitating the release of guanosine diphosphate (GDP). The amino and carboxyl termini, which contain receptor and beta gamma binding determinants, are disordered in the complex with GTP, but are organized into a compact microdomain on GDP hydrolysis. The amino terminus also forms extensive quaternary contacts with neighboring alpha subunits in the lattice, suggesting that multimers of alpha subunits or heterotrimers may play a role in signal transduction.

About this StructureAbout this Structure

1GDD is a Single protein structure of sequence from Rattus norvegicus with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Tertiary and quaternary structural changes in Gi alpha 1 induced by GTP hydrolysis., Mixon MB, Lee E, Coleman DE, Berghuis AM, Gilman AG, Sprang SR, Science. 1995 Nov 10;270(5238):954-60. PMID:7481799

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