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3ehs

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{{Seed}}
 
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[[Image:3ehs.png|left|200px]]
 
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==Crystal structure of the extracellular domain of human corticotropin releasing factor receptor type 1 (CRFR1)==
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The line below this paragraph, containing "STRUCTURE_3ehs", creates the "Structure Box" on the page.
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<StructureSection load='3ehs' size='340' side='right'caption='[[3ehs]], [[Resolution|resolution]] 2.76&Aring;' 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'>[[3ehs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EHS FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.76&#8491;</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=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></td></tr>
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{{STRUCTURE_3ehs| PDB=3ehs | 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=3ehs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ehs OCA], [https://pdbe.org/3ehs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ehs RCSB], [https://www.ebi.ac.uk/pdbsum/3ehs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ehs ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[https://www.uniprot.org/uniprot/CRFR1_HUMAN CRFR1_HUMAN] Receptor for corticotropin releasing factor (CRH). Shows high-affinity CRF binding. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.<ref>PMID:18801728</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eh/3ehs_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ehs ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The bimolecular interaction between corticotropin-releasing factor (CRF), a neuropeptide, and its type 1 receptor (CRFR1), a class B G-protein-coupled receptor (GPCR), is crucial for activation of the hypothalamic-pituitary-adrenal axis in response to stress, and has been a target of intense drug design for the treatment of anxiety, depression, and related disorders. As a class B GPCR, CRFR1 contains an N-terminal extracellular domain (ECD) that provides the primary ligand binding determinants. Here we present three crystal structures of the human CRFR1 ECD, one in a ligand-free form and two in distinct CRF-bound states. The CRFR1 ECD adopts the alpha-beta-betaalpha fold observed for other class B GPCR ECDs, but the N-terminal alpha-helix is significantly shorter and does not contact CRF. CRF adopts a continuous alpha-helix that docks in a hydrophobic surface of the ECD that is distinct from the peptide-binding site of other class B GPCRs, thereby providing a basis for the specificity of ligand recognition between CRFR1 and other class B GPCRs. The binding of CRF is accompanied by clamp-like conformational changes of two loops of the receptor that anchor the CRF C terminus, including the C-terminal amide group. These structural studies provide a molecular framework for understanding peptide binding and specificity by the CRF receptors as well as a template for designing potent and selective CRFR1 antagonists for therapeutic applications.
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===Crystal structure of the extracellular domain of human corticotropin releasing factor receptor type 1 (CRFR1)===
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Molecular recognition of corticotropin-releasing factor by its G-protein-coupled receptor CRFR1.,Pioszak AA, Parker NR, Suino-Powell K, Xu HE J Biol Chem. 2008 Nov 21;283(47):32900-12. Epub 2008 Sep 17. PMID:18801728<ref>PMID:18801728</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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The line below this paragraph, {{ABSTRACT_PUBMED_18801728}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3ehs" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18801728 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18801728}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia coli K-12]]
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3EHS is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli,_homo_sapiens Escherichia coli, homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EHS OCA].
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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==Reference==
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[[Category: Pioszak AA]]
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Molecular recognition of corticotropin releasing factor by its G protein-coupled receptor CRFR1., Pioszak AA, Parker NR, Suino-Powell K, Xu HE, J Biol Chem. 2008 Sep 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18801728 18801728]
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[[Category: Xu HE]]
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[[Category: Escherichia coli, homo sapiens]]
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[[Category: Pdbx_ordinal=, <PDBx:audit_author.]]
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[[Category: Alternative splicing]]
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[[Category: Cell membrane]]
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[[Category: Corticotropin releasing factor]]
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[[Category: Extracellular domain]]
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[[Category: G protein-coupled receptor]]
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[[Category: Glycoprotein]]
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[[Category: Mbp fusion]]
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[[Category: Membrane]]
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[[Category: Membrane protein]]
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[[Category: Periplasm]]
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[[Category: Phosphoprotein]]
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[[Category: Receptor]]
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[[Category: Scr fold]]
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[[Category: Sugar transport]]
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[[Category: Transducer]]
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[[Category: Transmembrane]]
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[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 3 20:05:35 2008''
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Current revision

Crystal structure of the extracellular domain of human corticotropin releasing factor receptor type 1 (CRFR1)

PDB ID 3ehs

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