1tnd

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(New page: 200px<br /><applet load="1tnd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tnd, resolution 2.2&Aring;" /> '''THE 2.2 ANGSTROMS CRY...)
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[[Image:1tnd.gif|left|200px]]<br /><applet load="1tnd" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1tnd, resolution 2.2&Aring;" />
caption="1tnd, resolution 2.2&Aring;" />
'''THE 2.2 ANGSTROMS CRYSTAL STRUCTURE OF TRANSDUCIN-ALPHA COMPLEXED WITH GTP GAMMA S'''<br />
'''THE 2.2 ANGSTROMS CRYSTAL STRUCTURE OF TRANSDUCIN-ALPHA COMPLEXED WITH GTP GAMMA S'''<br />
==Overview==
==Overview==
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The 2.2 A crystal structure of activated rod transducin, Gt alpha.GTP, gamma S, shows the bound GTP gamma S molecule occluded deep in a cleft, between a domain structurally homologous to small GTPases and a helical, domain unique to heterotrimeric G proteins. The structure, when combined, with biochemical and genetic studies, suggests: how an activated receptor, might open this cleft to allow nucleotide exchange; a mechanism for, GTP-induced changes in effector and receptor binding surfaces; and a, mechanism for GTPase activity not evident from previous data.
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The 2.2 A crystal structure of activated rod transducin, Gt alpha.GTP gamma S, shows the bound GTP gamma S molecule occluded deep in a cleft between a domain structurally homologous to small GTPases and a helical domain unique to heterotrimeric G proteins. The structure, when combined with biochemical and genetic studies, suggests: how an activated receptor might open this cleft to allow nucleotide exchange; a mechanism for GTP-induced changes in effector and receptor binding surfaces; and a mechanism for GTPase activity not evident from previous data.
==About this Structure==
==About this Structure==
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1TND 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, CAC and GSP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TND OCA].
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1TND 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>, <scene name='pdbligand=CAC:'>CAC</scene> and <scene name='pdbligand=GSP:'>GSP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TND 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: 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: CAC]]
[[Category: CAC]]
[[Category: GSP]]
[[Category: GSP]]
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[[Category: binding protein(gtp)]]
[[Category: binding protein(gtp)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:25:55 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:15:22 2008''

Revision as of 13:15, 21 February 2008


1tnd, resolution 2.2Å

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THE 2.2 ANGSTROMS CRYSTAL STRUCTURE OF TRANSDUCIN-ALPHA COMPLEXED WITH GTP GAMMA S

Overview

The 2.2 A crystal structure of activated rod transducin, Gt alpha.GTP gamma S, shows the bound GTP gamma S molecule occluded deep in a cleft between a domain structurally homologous to small GTPases and a helical domain unique to heterotrimeric G proteins. The structure, when combined with biochemical and genetic studies, suggests: how an activated receptor might open this cleft to allow nucleotide exchange; a mechanism for GTP-induced changes in effector and receptor binding surfaces; and a mechanism for GTPase activity not evident from previous data.

About this Structure

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

Reference

The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S., Noel JP, Hamm HE, Sigler PB, Nature. 1993 Dec 16;366(6456):654-63. PMID:8259210

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