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| | <StructureSection load='3sn6' size='340' side='right'caption='[[3sn6]], [[Resolution|resolution]] 3.20Å' scene=''> | | <StructureSection load='3sn6' size='340' side='right'caption='[[3sn6]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3sn6]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin], [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat], [https://en.wikipedia.org/wiki/Camelus_glama Camelus glama] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SN6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SN6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3sn6]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4], [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Lama_glama Lama glama] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SN6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SN6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P0G:8-[(1R)-2-{[1,1-DIMETHYL-2-(2-METHYLPHENYL)ETHYL]AMINO}-1-HYDROXYETHYL]-5-HYDROXY-2H-1,4-BENZOXAZIN-3(4H)-ONE'>P0G</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GNAS, GNAS1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN]), Gnb1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), GNG2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN]), ADRB2, ADRB2R, B2AR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P0G:8-[(1R)-2-{[1,1-DIMETHYL-2-(2-METHYLPHENYL)ETHYL]AMINO}-1-HYDROXYETHYL]-5-HYDROXY-2H-1,4-BENZOXAZIN-3(4H)-ONE'>P0G</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3sn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sn6 OCA], [https://pdbe.org/3sn6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sn6 RCSB], [https://www.ebi.ac.uk/pdbsum/3sn6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sn6 ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3sn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sn6 OCA], [https://pdbe.org/3sn6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sn6 RCSB], [https://www.ebi.ac.uk/pdbsum/3sn6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sn6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/ENLYS_BPT4 ENLYS_BPT4]] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.<ref>PMID:22389108</ref> [[https://www.uniprot.org/uniprot/GNAS2_BOVIN GNAS2_BOVIN]] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(s) protein is involved in hormonal regulation of adenylate cyclase: it activates the cyclase in response to beta-adrenergic stimuli. [[https://www.uniprot.org/uniprot/GBG2_BOVIN GBG2_BOVIN]] Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. [[https://www.uniprot.org/uniprot/GBB1_RAT GBB1_RAT]] Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
| + | [https://www.uniprot.org/uniprot/GNAS2_BOVIN GNAS2_BOVIN] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(s) protein is involved in hormonal regulation of adenylate cyclase: it activates the cyclase in response to beta-adrenergic stimuli. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bovin]] | + | [[Category: Bos taurus]] |
| - | [[Category: Buffalo rat]] | + | [[Category: Escherichia virus T4]] |
| - | [[Category: Camelus glama]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | + | [[Category: Lama glama]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysozyme]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Caffrey, M]] | + | [[Category: Caffrey M]] |
| - | [[Category: Calinski, D]] | + | [[Category: Calinski D]] |
| - | [[Category: Chae, P S]] | + | [[Category: Chae PS]] |
| - | [[Category: Chung, K Y]] | + | [[Category: Chung KY]] |
| - | [[Category: DeVree, B T]] | + | [[Category: DeVree BT]] |
| - | [[Category: Gellman, S H]] | + | [[Category: Gellman SH]] |
| - | [[Category: Kobilka, B K]] | + | [[Category: Kobilka BK]] |
| - | [[Category: Kobilka, T S]] | + | [[Category: Kobilka TS]] |
| - | [[Category: Kruse, A C]] | + | [[Category: Kruse AC]] |
| - | [[Category: Lyons, J A]] | + | [[Category: Lyons JA]] |
| - | [[Category: Mathiesen, J M]] | + | [[Category: Mathiesen JM]] |
| - | [[Category: Pardon, E]] | + | [[Category: Pardon E]] |
| - | [[Category: Rasmussen, S G.F]] | + | [[Category: Rasmussen SGF]] |
| - | [[Category: Shah, S T.A]] | + | [[Category: Shah STA]] |
| - | [[Category: Skiniotis, G]] | + | [[Category: Skiniotis G]] |
| - | [[Category: Steyaert, J]] | + | [[Category: Steyaert J]] |
| - | [[Category: Sunahara, R K]] | + | [[Category: Sunahara RK]] |
| - | [[Category: Thian, F S]] | + | [[Category: Thian FS]] |
| - | [[Category: Weis, W I]] | + | [[Category: Weis WI]] |
| - | [[Category: Zou, Y]] | + | [[Category: Zou Y]] |
| - | [[Category: G protein signaling]]
| + | |
| - | [[Category: G protein-coupled receptor]]
| + | |
| - | [[Category: Gpcr]]
| + | |
| - | [[Category: Nanobody]]
| + | |
| - | [[Category: Seven transmembrane receptor]]
| + | |
| - | [[Category: Signal transduction]]
| + | |
| - | [[Category: Signaling protein-hydrolase complex]]
| + | |
| Structural highlights
Function
GNAS2_BOVIN Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(s) protein is involved in hormonal regulation of adenylate cyclase: it activates the cyclase in response to beta-adrenergic stimuli.
Publication Abstract from PubMed
G protein-coupled receptors (GPCRs) are responsible for the majority of cellular responses to hormones and neurotransmitters as well as the senses of sight, olfaction and taste. The paradigm of GPCR signalling is the activation of a heterotrimeric GTP binding protein (G protein) by an agonist-occupied receptor. The beta(2) adrenergic receptor (beta(2)AR) activation of Gs, the stimulatory G protein for adenylyl cyclase, has long been a model system for GPCR signalling. Here we present the crystal structure of the active state ternary complex composed of agonist-occupied monomeric beta(2)AR and nucleotide-free Gs heterotrimer. The principal interactions between the beta(2)AR and Gs involve the amino- and carboxy-terminal alpha-helices of Gs, with conformational changes propagating to the nucleotide-binding pocket. The largest conformational changes in the beta(2)AR include a 14 A outward movement at the cytoplasmic end of transmembrane segment 6 (TM6) and an alpha-helical extension of the cytoplasmic end of TM5. The most surprising observation is a major displacement of the alpha-helical domain of Galphas relative to the Ras-like GTPase domain. This crystal structure represents the first high-resolution view of transmembrane signalling by a GPCR.
Crystal structure of the beta2 adrenergic receptor-Gs protein complex.,Rasmussen SG, DeVree BT, Zou Y, Kruse AC, Chung KY, Kobilka TS, Thian FS, Chae PS, Pardon E, Calinski D, Mathiesen JM, Shah ST, Lyons JA, Caffrey M, Gellman SH, Steyaert J, Skiniotis G, Weis WI, Sunahara RK, Kobilka BK Nature. 2011 Jul 19;477(7366):549-55. doi: 10.1038/nature10361. PMID:21772288[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rasmussen SG, DeVree BT, Zou Y, Kruse AC, Chung KY, Kobilka TS, Thian FS, Chae PS, Pardon E, Calinski D, Mathiesen JM, Shah ST, Lyons JA, Caffrey M, Gellman SH, Steyaert J, Skiniotis G, Weis WI, Sunahara RK, Kobilka BK. Crystal structure of the beta2 adrenergic receptor-Gs protein complex. Nature. 2011 Jul 19;477(7366):549-55. doi: 10.1038/nature10361. PMID:21772288 doi:10.1038/nature10361
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