2low

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==Solution structure of AR55 in 50% HFIP==
==Solution structure of AR55 in 50% HFIP==
<StructureSection load='2low' size='340' side='right' caption='[[2low]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''>
<StructureSection load='2low' size='340' side='right' caption='[[2low]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2low]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LOW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LOW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2low]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LOW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LOW FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lot|2lot]], [[2lou|2lou]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lot|2lot]], [[2lou|2lou]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">APLNR, AGTRL1, APJ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2low FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2low OCA], [http://pdbe.org/2low PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2low RCSB], [http://www.ebi.ac.uk/pdbsum/2low PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2low ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2low FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2low OCA], [http://pdbe.org/2low PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2low RCSB], [http://www.ebi.ac.uk/pdbsum/2low PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/APJ_HUMAN APJ_HUMAN]] Receptor for apelin coupled to G proteins that inhibit adenylate cyclase activity. Alternative coreceptor with CD4 for HIV-1 infection; may be involved in the development of AIDS dementia.
[[http://www.uniprot.org/uniprot/APJ_HUMAN APJ_HUMAN]] Receptor for apelin coupled to G proteins that inhibit adenylate cyclase activity. Alternative coreceptor with CD4 for HIV-1 infection; may be involved in the development of AIDS dementia.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Detergent micelles are frequently employed as membrane mimetics for solution-state membrane protein nuclear magnetic resonance spectroscopy. Here we compare topology, structure, ps-ns time-scale dynamics, and hydrodynamics of a model protein with one transmembrane (TM) segment (residues 1-55 of the apelin receptor, APJ, a G-protein-coupled receptor) in three distinct, commonly used micellar environments. In each environment, two solvent-protected helical segments connected by a solvent-exposed kink were observed. The break in helical character at the kink was maintained in a helix-stabilizing fluorinated alcohol environment, implying that this structural feature is inherent. Molecular dynamics simulations also substantiate favorable self-assembly of compact protein-micelle complexes with a more dynamic, solvent-exposed kink. Despite the observed similarity in TM segment behavior, micelle-dependent differences were clear in the structure, dynamics, and compactness of the 30-residue, extramembrane N-terminal tail of the protein. This would affect intermolecular interactions and, correspondingly, the functional state of the membrane protein.
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Preserved Transmembrane Segment Topology, Structure, and Dynamics in Disparate Micellar Environments.,Langelaan DN, Pandey A, Sarker M, Rainey JK J Phys Chem Lett. 2017 May 12:2381-2386. doi: 10.1021/acs.jpclett.7b00867. PMID:28492329<ref>PMID:28492329</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 2low" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
 
[[Category: Langelaan, D N]]
[[Category: Langelaan, D N]]
[[Category: Rainey, J K]]
[[Category: Rainey, J K]]
[[Category: Membrane protein]]
[[Category: Membrane protein]]

Revision as of 07:24, 24 May 2017

Solution structure of AR55 in 50% HFIP

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