2yx8: Difference between revisions
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==Crystal structure of the extracellular domain of human RAMP1== | ==Crystal structure of the extracellular domain of human RAMP1== | ||
<StructureSection load='2yx8' size='340' side='right' caption='[[2yx8]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='2yx8' size='340' side='right' caption='[[2yx8]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
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</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAMP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAMP1 ([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=2yx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yx8 OCA], [http://pdbe.org/2yx8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yx8 RCSB], [http://www.ebi.ac.uk/pdbsum/2yx8 PDBsum], [http://www.topsan.org/Proteins/RSGI/2yx8 TOPSAN]</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=2yx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yx8 OCA], [http://pdbe.org/2yx8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yx8 RCSB], [http://www.ebi.ac.uk/pdbsum/2yx8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yx8 ProSAT], [http://www.topsan.org/Proteins/RSGI/2yx8 TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yx/2yx8_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yx/2yx8_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 12:17, 17 October 2018
Crystal structure of the extracellular domain of human RAMP1Crystal structure of the extracellular domain of human RAMP1
Structural highlights
Function[RAMP1_HUMAN] Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for calcitonin-gene-related peptide (CGRP) together with CALCRL.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedReceptor activity-modifying protein (RAMP) 1 forms a heterodimer with calcitonin receptor-like receptor (CRLR) and regulates its transport to the cell surface. The CRLR.RAMP1 heterodimer functions as a specific receptor for calcitonin gene-related peptide (CGRP). Here, we report the crystal structure of the human RAMP1 extracellular domain. The RAMP1 structure is a three-helix bundle that is stabilized by three disulfide bonds. The RAMP1 residues important for cell-surface expression of the CRLR.RAMP1 heterodimer are clustered to form a hydrophobic patch on the molecular surface. The hydrophobic patch is located near the tryptophan residue essential for binding of the CGRP antagonist, BIBN4096BS. These results suggest that the hydrophobic patch participates in the interaction with CRLR and the formation of the ligand-binding pocket when it forms the CRLR.RAMP1 heterodimer. Crystal structure of the human receptor activity-modifying protein 1 extracellular domain.,Kusano S, Kukimoto-Niino M, Akasaka R, Toyama M, Terada T, Shirouzu M, Shindo T, Yokoyama S Protein Sci. 2008 Nov;17(11):1907-14. Epub 2008 Aug 25. PMID:18725456[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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