3ehs: Difference between revisions

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{{Seed}}
[[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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<StructureSection load='3ehs' size='340' side='right'caption='[[3ehs]], [[Resolution|resolution]] 2.76&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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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</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>
{{STRUCTURE_3ehs|  PDB=3ehs  |  SCENE=  }}
<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>
</table>
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eh/3ehs_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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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== Publication Abstract from PubMed ==
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.


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


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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(as it appears on PubMed at http://www.pubmed.gov), where 18801728 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_18801728}}
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</StructureSection>
==About this Structure==
[[Category: Escherichia coli K-12]]
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].
[[Category: Homo sapiens]]
 
[[Category: Large Structures]]
==Reference==
[[Category: Pioszak AA]]
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]
[[Category: Xu HE]]
[[Category: Escherichia coli, homo sapiens]]
[[Category: Pioszak, A A.]]
[[Category: Xu, H E.]]
[[Category: Alternative splicing]]
[[Category: Cell membrane]]
[[Category: Corticotropin releasing factor]]
[[Category: Extracellular domain]]
[[Category: G protein-coupled receptor]]
[[Category: Glycoprotein]]
[[Category: Mbp fusion]]
[[Category: Membrane]]
[[Category: Membrane protein]]
[[Category: Periplasm]]
[[Category: Phosphoprotein]]
[[Category: Receptor]]
[[Category: Scr fold]]
[[Category: Sugar transport]]
[[Category: Transducer]]
[[Category: Transmembrane]]
[[Category: Transport]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 10 15:29:54 2008''