Entry | Database: PDB / ID: 4ku8 |
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Title | Structures of PKGI Reveal a cGMP-Selective Activation Mechanism |
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Components | cGMP-dependent Protein Kinase 1 |
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Keywords | SIGNALING PROTEIN / cyclic nucleotide binding domain / cGMP |
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Function / homology | Function and homology information
negative regulation of inositol phosphate biosynthetic process / negative regulation of glutamate secretion / cGMP-dependent protein kinase / cGMP-dependent protein kinase activity / cell growth involved in cardiac muscle cell development / regulation of testosterone biosynthetic process / collateral sprouting / negative regulation of vascular associated smooth muscle cell migration / negative regulation of platelet aggregation / relaxation of vascular associated smooth muscle ...negative regulation of inositol phosphate biosynthetic process / negative regulation of glutamate secretion / cGMP-dependent protein kinase / cGMP-dependent protein kinase activity / cell growth involved in cardiac muscle cell development / regulation of testosterone biosynthetic process / collateral sprouting / negative regulation of vascular associated smooth muscle cell migration / negative regulation of platelet aggregation / relaxation of vascular associated smooth muscle / positive regulation of circadian rhythm / Rap1 signalling / cGMP-mediated signaling / mitogen-activated protein kinase p38 binding / regulation of GTPase activity / dendrite development / spermatid development / cGMP effects / negative regulation of vascular associated smooth muscle cell proliferation / calcium channel regulator activity / cGMP binding / forebrain development / cerebellum development / acrosomal vesicle / neuron migration / sarcolemma / Ca2+ pathway / positive regulation of cytosolic calcium ion concentration / actin cytoskeleton organization / protein kinase activity / protein phosphorylation / protein serine kinase activity / Golgi apparatus / signal transduction / nucleoplasm / ATP binding / identical protein binding / plasma membrane / cytosol / cytoplasmSimilarity search - Function cGMP-dependent protein kinase, N-terminal coiled-coil domain / Coiled-coil N-terminus of cGMP-dependent protein kinase / cGMP-dependent kinase / cGMP-dependent protein kinase, catalytic domain / Cyclic nucleotide-binding domain signature 2. / Cyclic nucleotide-binding domain signature 1. / Cyclic nucleotide-binding, conserved site / Cyclic nucleotide-monophosphate binding domain / Cyclic nucleotide-binding domain / cAMP/cGMP binding motif profile. ...cGMP-dependent protein kinase, N-terminal coiled-coil domain / Coiled-coil N-terminus of cGMP-dependent protein kinase / cGMP-dependent kinase / cGMP-dependent protein kinase, catalytic domain / Cyclic nucleotide-binding domain signature 2. / Cyclic nucleotide-binding domain signature 1. / Cyclic nucleotide-binding, conserved site / Cyclic nucleotide-monophosphate binding domain / Cyclic nucleotide-binding domain / cAMP/cGMP binding motif profile. / Cyclic nucleotide-binding domain / Cyclic nucleotide-binding domain superfamily / Extension to Ser/Thr-type protein kinases / Jelly Rolls / AGC-kinase, C-terminal / AGC-kinase C-terminal domain profile. / RmlC-like jelly roll fold / Jelly Rolls / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Sandwich / Mainly BetaSimilarity search - Domain/homology |
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Biological species | Homo sapiens (human) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.994 Å |
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Authors | Huang, G.Y. / Kim, J.J. / Reger, A.S. / Lorenz, R. / Moon, E.W. / Casteel, D.E. / Sankaran, B. / Herberg, F.W. / Kim, C. |
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Citation | Journal: Structure / Year: 2014 Title: Structural Basis for Cyclic-Nucleotide Selectivity and cGMP-Selective Activation of PKG I. Authors: Huang, G.Y. / Kim, J.J. / Reger, A.S. / Lorenz, R. / Moon, E.W. / Zhao, C. / Casteel, D.E. / Bertinetti, D. / Vanschouwen, B. / Selvaratnam, R. / Pflugrath, J.W. / Sankaran, B. / Melacini, G. ...Authors: Huang, G.Y. / Kim, J.J. / Reger, A.S. / Lorenz, R. / Moon, E.W. / Zhao, C. / Casteel, D.E. / Bertinetti, D. / Vanschouwen, B. / Selvaratnam, R. / Pflugrath, J.W. / Sankaran, B. / Melacini, G. / Herberg, F.W. / Kim, C. |
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History | Deposition | May 21, 2013 | Deposition site: RCSB / Processing site: RCSB |
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Revision 1.0 | Jan 15, 2014 | Provider: repository / Type: Initial release |
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Revision 1.1 | Jan 29, 2014 | Group: Database references |
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Revision 1.2 | Nov 15, 2017 | Group: Refinement description / Category: software |
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Revision 1.3 | Feb 28, 2024 | Group: Data collection / Database references / Derived calculations Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id |
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