3aqe
From Proteopedia
(Difference between revisions)
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==Crystal structure of the extracellular domain of human RAMP2== | ==Crystal structure of the extracellular domain of human RAMP2== | ||
<StructureSection load='3aqe' size='340' side='right' caption='[[3aqe]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3aqe' size='340' side='right' caption='[[3aqe]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3aqe]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3aqe]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AQE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AQE FirstGlance]. <br> |
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3aqf|3aqf]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3aqf|3aqf]]</td></tr> | ||
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAMP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAMP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
- | <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=3aqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aqe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aqe RCSB], [http://www.ebi.ac.uk/pdbsum/3aqe PDBsum]</span></td></tr> | + | <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=3aqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aqe OCA], [http://pdbe.org/3aqe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3aqe RCSB], [http://www.ebi.ac.uk/pdbsum/3aqe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3aqe ProSAT]</span></td></tr> |
</table> | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/RAMP2_HUMAN RAMP2_HUMAN]] Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for adrenomedullin (AM) together with CALCRL.<ref>PMID:22102369</ref> <ref>PMID:9620797</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
+ | <div class="pdbe-citations 3aqe" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Human]] |
[[Category: Kukimoto-Niino, M]] | [[Category: Kukimoto-Niino, M]] | ||
[[Category: Kusano, S]] | [[Category: Kusano, S]] |
Revision as of 11:47, 4 August 2016
Crystal structure of the extracellular domain of human RAMP2
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Categories: Human | Kukimoto-Niino, M | Kusano, S | Shindo, T | Shirouzu, M | Yokoyama, S | Adrenomedullin | Cell membrane | Cgrp | Clr | Disease | Endoplasmic reticulum | Gpcr | Helix bundle | Neovascularization | Trafficking | Transmembrane | Transport protein