3aqf
From Proteopedia
(Difference between revisions)
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==Crystal structure of the human CRLR/RAMP2 extracellular complex== | ==Crystal structure of the human CRLR/RAMP2 extracellular complex== | ||
- | <StructureSection load='3aqf' size='340' side='right' caption='[[3aqf]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='3aqf' size='340' side='right'caption='[[3aqf]], [[Resolution|resolution]] 2.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3aqf]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3aqf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AQF 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">[[3aqe|3aqe]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3aqe|3aqe]]</div></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAMP2 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAMP2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CALCRL, CGRPR ([https://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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3aqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aqf OCA], [https://pdbe.org/3aqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aqf RCSB], [https://www.ebi.ac.uk/pdbsum/3aqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aqf ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://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> [[https://www.uniprot.org/uniprot/CALRL_HUMAN CALRL_HUMAN]] Receptor for calcitonin-gene-related peptide (CGRP) together with RAMP1 and receptor for adrenomedullin together with RAMP3 (By similarity). Receptor for adrenomedullin together with RAMP2. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.<ref>PMID:22102369</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Kukimono-Niino, M]] | [[Category: Kukimono-Niino, M]] | ||
[[Category: Kusano, S]] | [[Category: Kusano, S]] |
Revision as of 15:01, 29 December 2021
Crystal structure of the human CRLR/RAMP2 extracellular complex
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Categories: Human | Large Structures | Kukimono-Niino, M | Kusano, S | Shindo, T | Shirouzu, M | Yokoyama, S | Adrenomedullin | Am-receptor | Cgrp | Clr | Co-activating receptor for adrenomedullin | Disease | Endoplasmic reticulum | Gpcr | Neovascularization | Trafficking | Transmembrane | Transport protein-membrane protein complex