1l4t

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[[Image:1l4t.png|left|200px]]
 
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==SOLUTION NMR STRUCTURE OF THE CCK2E3==
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The line below this paragraph, containing "STRUCTURE_1l4t", creates the "Structure Box" on the page.
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<StructureSection load='1l4t' size='340' side='right'caption='[[1l4t]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1l4t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L4T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L4T FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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{{STRUCTURE_1l4t| PDB=1l4t | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l4t OCA], [https://pdbe.org/1l4t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l4t RCSB], [https://www.ebi.ac.uk/pdbsum/1l4t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l4t ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GASR_HUMAN GASR_HUMAN] Receptor for gastrin and cholecystokinin. The CKK-B receptors occur throughout the central nervous system where they modulate anxiety, analgesia, arousal, and neuroleptic activity. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.<ref>PMID:8349705</ref> <ref>PMID:8185170</ref> <ref>PMID:7848914</ref> <ref>PMID:10913157</ref> <ref>PMID:11495676</ref> <ref>PMID:8221657</ref> Isoform 2 is constitutively activated and may regulate cancer cell proliferation via a gastrin-independent mechanism.<ref>PMID:8349705</ref> <ref>PMID:8185170</ref> <ref>PMID:7848914</ref> <ref>PMID:10913157</ref> <ref>PMID:11495676</ref> <ref>PMID:8221657</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structure of the third extracellular loop of the human cholecystokinin-2 receptor, CCK2-R(352-379), and its interactions with the C-terminal octapeptide of cholecystokinin (CCK-8) have been determined by high-resolution NMR and computer simulations. In the presence of dodecylphosphocholine micelles, the structure of the receptor fragment consisted of three helices, with the first and third corresponding to residues of the extracellular ends of transmembrane helices (TM) 6 and 7, respectively. The central, extracellular helix, consisting of residues 363-368, was found to be closely associated with the membrane mimetic used during the spectroscopic studies and molecular dynamics (MD) simulations. Upon titration of CCK-8 to the receptor domain, chemical shift perturbation and intermolecular NOEs (Trp30, Met31 of CCK-8 and P371, F374 of CCK2-R) indicated the formation of a stable complex and specific ligand/receptor interactions. Using the NOE-generated intermolecular contact points, extensive MD simulations of CCK-8 bound to the CCK2 receptor were carried out. The results, with CCK-8 in close proximity to TM7, differ from previous structural studies of CCK-8 association with CCK1-R, in which the ligand formed a number of interactions with TM6. These differences may play a role in the ligand specificity displayed by the CCK1 and CCK2 receptor subtypes.
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===SOLUTION NMR STRUCTURE OF THE CCK2E3===
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Intermolecular interactions between cholecystokinin-8 and the third extracellular loop of the cholecystokinin-2 receptor.,Giragossian C, Mierke DF Biochemistry. 2002 Apr 9;41(14):4560-6. PMID:11926817<ref>PMID:11926817</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1l4t" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11926817 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11926817}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Homo sapiens]]
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1L4T is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L4T OCA].
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[[Category: Large Structures]]
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[[Category: Giragossian C]]
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==Reference==
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[[Category: Mierke DF]]
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Intermolecular interactions between cholecystokinin-8 and the third extracellular loop of the cholecystokinin-2 receptor., Giragossian C, Mierke DF, Biochemistry. 2002 Apr 9;41(14):4560-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11926817 11926817]
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[[Category: Single protein]]
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[[Category: Giragossian, C.]]
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[[Category: Mierke, D F.]]
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[[Category: Hormone/growth factor receptor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:42:10 2008''
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Current revision

SOLUTION NMR STRUCTURE OF THE CCK2E3

PDB ID 1l4t

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