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| [[Image:2hlb.gif|left|200px]]
| | <table cellpadding='5'><tr><td style='background-color: yellow;border:2px solid black;font-size:150%;'> |
| | | NOTE: This structure was removed. For additional information see '''2012, January:''' at [[Retractions and Fraud]].</td></tr></table> |
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| {{STRUCTURE_2hlb| PDB=2hlb | SCENE= }}
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| '''A Structural Basis for Nucleotide Exchange on G-alpha-i Subunits and Receptor Coupling Specificity''' | |
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| ==Overview==
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| Heterotrimeric G proteins are molecular switches that relay information intracellularly in response to various extracellular signals. How ligand-activated G protein-coupled receptors act at a distance to exert exchange activity on the Galpha nucleotide binding pocket is poorly understood. Here we describe the synergistic action of two peptides: one from the third intracellular loop of the D2 dopamine receptor (D2N), and a second, Galpha.GDP-binding peptide (KB-752) that mimics the proposed role of Gbetagamma in receptor-promoted nucleotide exchange. The structure of both peptides in complex with Galpha(i1) suggests that conformational changes in the beta3/alpha2 loop and beta6 strand act in concert for efficient nucleotide exchange. Two key residues in the alpha4 helix were found to define a receptor/Galpha(i) coupling specificity determinant.
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| ==About this Structure==
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| 2HLB is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HLB OCA].
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| ==Reference==
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| Structural basis for nucleotide exchange on G alpha i subunits and receptor coupling specificity., Johnston CA, Siderovski DP, Proc Natl Acad Sci U S A. 2007 Feb 6;104(6):2001-6. Epub 2007 Jan 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17264214 17264214]
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| [[Category: Homo sapiens]] | |
| [[Category: Protein complex]]
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| [[Category: Johnston, C A.]]
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| [[Category: Siderovski, D P.]]
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| [[Category: Watts, V J.]]
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| [[Category: Protein:peptide complex]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:25:26 2008''
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