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| [[Image:3c4z.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_3c4z| PDB=3c4z | SCENE= }} | | {{STRUCTURE_3c4z| PDB=3c4z | SCENE= }} |
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| '''Crystal structure of G protein coupled receptor kinase 1 bound to ADP and magnesium chloride at 1.84A'''
| | ===Crystal structure of G protein coupled receptor kinase 1 bound to ADP and magnesium chloride at 1.84A=== |
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| ==Overview==
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| G protein-coupled receptor (GPCR) kinases (GRKs) phosphorylate activated heptahelical receptors, leading to their uncoupling from G proteins. Here we report six crystal structures of rhodopsin kinase (GRK1), revealing not only three distinct nucleotide-binding states of a GRK but also two key structural elements believed to be involved in the recognition of activated GPCRs. The first is the C-terminal extension of the kinase domain, which was observed in all nucleotide-bound GRK1 structures. The second is residues 5-30 of the N terminus, observed in one of the GRK1.(Mg(2+))(2).ATP structures. The N terminus was also clearly phosphorylated, leading to the identification of two novel phosphorylation sites by mass spectral analysis. Co-localization of the N terminus and the C-terminal extension near the hinge of the kinase domain suggests that activated GPCRs stimulate kinase activity by binding to this region to facilitate full closure of the kinase domain.
| | The line below this paragraph, {{ABSTRACT_PUBMED_18339619}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18339619 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18339619}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Serine/threonine-protein kinase]] | | [[Category: Serine/threonine-protein kinase]] |
| [[Category: Transferase]] | | [[Category: Transferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 22:36:48 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:46:09 2008'' |