6cm4: Difference between revisions
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<StructureSection load='6cm4' size='340' side='right'caption='[[6cm4]], [[Resolution|resolution]] 2.87Å' scene=''> | <StructureSection load='6cm4' size='340' side='right'caption='[[6cm4]], [[Resolution|resolution]] 2.87Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6cm4]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6cm4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6c38 6c38]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CM4 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8NU:3-[2-[4-(6-fluoranyl-1,2-benzoxazol-3-yl)piperidin-1-yl]ethyl]-2-methyl-6,7,8,9-tetrahydropyrido[1,2-a]pyrimidin-4-one'>8NU</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.867Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8NU:3-[2-[4-(6-fluoranyl-1,2-benzoxazol-3-yl)piperidin-1-yl]ethyl]-2-methyl-6,7,8,9-tetrahydropyrido[1,2-a]pyrimidin-4-one'>8NU</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=6cm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cm4 OCA], [https://pdbe.org/6cm4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cm4 RCSB], [https://www.ebi.ac.uk/pdbsum/6cm4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cm4 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Disease == | == Disease == | ||
[ | [https://www.uniprot.org/uniprot/DRD2_HUMAN DRD2_HUMAN] Myoclonic dystonia 11. The gene represented in this entry may be involved in disease pathogenesis. DRD2 mutations in myoclonic dystonia patients are rare, and their contribution to disease phenotype is unclear (PubMed:10716258). | ||
== 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/DRD2_HUMAN DRD2_HUMAN] Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase (By similarity).<ref>PMID:21645528</ref> <ref>PMID:17264214</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Dopamine receptor|Dopamine receptor]] | *[[Dopamine receptor 3D structures|Dopamine receptor 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia virus T4]] | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Che T]] | |||
[[Category: Che | [[Category: Levit A]] | ||
[[Category: Levit | [[Category: Roth BL]] | ||
[[Category: Roth | [[Category: Shoichet BK]] | ||
[[Category: Shoichet | [[Category: Wacker D]] | ||
[[Category: Wacker | [[Category: Wang S]] | ||
[[Category: Wang | |||
Latest revision as of 18:07, 4 October 2023
Structure of the D2 Dopamine Receptor Bound to the Atypical Antipsychotic Drug RisperidoneStructure of the D2 Dopamine Receptor Bound to the Atypical Antipsychotic Drug Risperidone
Structural highlights
DiseaseDRD2_HUMAN Myoclonic dystonia 11. The gene represented in this entry may be involved in disease pathogenesis. DRD2 mutations in myoclonic dystonia patients are rare, and their contribution to disease phenotype is unclear (PubMed:10716258). FunctionENLYS_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.[1] DRD2_HUMAN Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase (By similarity).[2] [3] Publication Abstract from PubMedDopamine is a neurotransmitter that has been implicated in processes as diverse as reward, addiction, control of coordinated movement, metabolism and hormonal secretion. Correspondingly, dysregulation of the dopaminergic system has been implicated in diseases such as schizophrenia, Parkinson's disease, depression, attention deficit hyperactivity disorder, nausea and vomiting, among others. Dopamine's actions are mediated by a family of five G-protein coupled receptors (GPCRs) (viz. D1, D2, D3, D4 and D5)(1). The D2 dopamine receptor (DRD2) is the primary target for both typical(2) and atypical(3,4) antipsychotic drugs, and for Parkinson's disease drugs. Unfortunately, many drugs targeting DRD2 frequently cause serious and potentially life-threatening side effects due to promiscuous activities against related receptors(4,5). Accordingly, a molecular understanding of DRD2 structure and function could provide a template for the design of safer and more effective medications. Here we provide the crystal structure of DRD2 in complex with the widely prescribed atypical antipsychotic drug risperidone. The DRD2-risperidone structure reveals an unexpected mode of antipsychotic drug binding to dopamine receptors, and illuminates structural determinants essential for the actions of risperidone and related drugs at DRD2. Structure of the D2 dopamine receptor bound to the atypical antipsychotic drug risperidone.,Wang S, Che T, Levit A, Shoichet BK, Wacker D, Roth BL Nature. 2018 Jan 24. pii: nature25758. doi: 10.1038/nature25758. PMID:29466326[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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