1y3a
From Proteopedia
(New page: 200px<br /> <applet load="1y3a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y3a, resolution 2.5Å" /> '''Structure of G-Alpha...) |
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| - | [[Image:1y3a.gif|left|200px]]<br /> | + | [[Image:1y3a.gif|left|200px]]<br /><applet load="1y3a" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1y3a" size=" | + | |
caption="1y3a, resolution 2.5Å" /> | caption="1y3a, resolution 2.5Å" /> | ||
'''Structure of G-Alpha-I1 bound to a GDP-selective peptide provides insight into guanine nucleotide exchange'''<br /> | '''Structure of G-Alpha-I1 bound to a GDP-selective peptide provides insight into guanine nucleotide exchange'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Heterotrimeric G proteins are molecular switches that regulate numerous | + | Heterotrimeric G proteins are molecular switches that regulate numerous signaling pathways involved in cellular physiology. This characteristic is achieved by the adoption of two principal states: an inactive, GDP bound state and an active, GTP bound state. Under basal conditions, G proteins exist in the inactive, GDP bound state; thus, nucleotide exchange is crucial to the onset of signaling. Despite our understanding of G protein signaling pathways, the mechanism of nucleotide exchange remains elusive. We employed phage display technology to identify nucleotide state-dependent Galpha binding peptides. Herein, we report a GDP-selective Galpha binding peptide, KB-752, that enhances spontaneous nucleotide exchange of Galpha(i) subunits. Structural determination of the Galpha(i1)/peptide complex reveals unique changes in the Galpha switch regions predicted to enhance nucleotide exchange by creating a GDP dissociation route. Our results cast light onto a potential mechanism by which Galpha subunits adopt a conformation suitable for nucleotide exchange. |
==About this Structure== | ==About this Structure== | ||
| - | 1Y3A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with GDP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1Y3A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y3A OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Blaesius, R.]] | [[Category: Blaesius, R.]] | ||
| - | [[Category: Bodor, E | + | [[Category: Bodor, E T.]] |
[[Category: Fredericks, Z.]] | [[Category: Fredericks, Z.]] | ||
| - | [[Category: Harden, T | + | [[Category: Harden, T K.]] |
| - | [[Category: Jezyk, M | + | [[Category: Jezyk, M R.]] |
| - | [[Category: Johnston, C | + | [[Category: Johnston, C A.]] |
| - | [[Category: Jones, M | + | [[Category: Jones, M B.]] |
| - | [[Category: Ramer, J | + | [[Category: Ramer, J K.]] |
| - | [[Category: Siderovski, D | + | [[Category: Siderovski, D P.]] |
[[Category: Sondek, J.]] | [[Category: Sondek, J.]] | ||
| - | [[Category: Watts, V | + | [[Category: Watts, V J.]] |
| - | [[Category: Willard, F | + | [[Category: Willard, F S.]] |
[[Category: GDP]] | [[Category: GDP]] | ||
[[Category: protein-peptide complex]] | [[Category: protein-peptide complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:01:24 2008'' |
Revision as of 14:01, 21 February 2008
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Structure of G-Alpha-I1 bound to a GDP-selective peptide provides insight into guanine nucleotide exchange
Overview
Heterotrimeric G proteins are molecular switches that regulate numerous signaling pathways involved in cellular physiology. This characteristic is achieved by the adoption of two principal states: an inactive, GDP bound state and an active, GTP bound state. Under basal conditions, G proteins exist in the inactive, GDP bound state; thus, nucleotide exchange is crucial to the onset of signaling. Despite our understanding of G protein signaling pathways, the mechanism of nucleotide exchange remains elusive. We employed phage display technology to identify nucleotide state-dependent Galpha binding peptides. Herein, we report a GDP-selective Galpha binding peptide, KB-752, that enhances spontaneous nucleotide exchange of Galpha(i) subunits. Structural determination of the Galpha(i1)/peptide complex reveals unique changes in the Galpha switch regions predicted to enhance nucleotide exchange by creating a GDP dissociation route. Our results cast light onto a potential mechanism by which Galpha subunits adopt a conformation suitable for nucleotide exchange.
About this Structure
1Y3A is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of Galpha(i1) bound to a GDP-selective peptide provides insight into guanine nucleotide exchange., Johnston CA, Willard FS, Jezyk MR, Fredericks Z, Bodor ET, Jones MB, Blaesius R, Watts VJ, Harden TK, Sondek J, Ramer JK, Siderovski DP, Structure. 2005 Jul;13(7):1069-80. PMID:16004878
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