4nc3: Difference between revisions
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==Crystal structure of the 5-HT2B receptor solved using serial femtosecond crystallography in lipidic cubic phase.== | ==Crystal structure of the 5-HT2B receptor solved using serial femtosecond crystallography in lipidic cubic phase.== | ||
<StructureSection load='4nc3' size='340' side='right' caption='[[4nc3]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='4nc3' size='340' side='right' caption='[[4nc3]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ib4|4ib4]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ib4|4ib4]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">5HT2B_HUMAN, cybC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">5HT2B_HUMAN, cybC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=4nc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nc3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nc3 RCSB], [http://www.ebi.ac.uk/pdbsum/4nc3 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=4nc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nc3 OCA], [http://pdbe.org/4nc3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nc3 RCSB], [http://www.ebi.ac.uk/pdbsum/4nc3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nc3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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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 4nc3" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[5-hydroxytryptamine receptor|5-hydroxytryptamine receptor]] | |||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 08:28, 5 August 2016
Crystal structure of the 5-HT2B receptor solved using serial femtosecond crystallography in lipidic cubic phase.Crystal structure of the 5-HT2B receptor solved using serial femtosecond crystallography in lipidic cubic phase.
Structural highlights
Function[5HT2B_HUMAN] This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Plays a role in the regulation of impulsive behavior. Publication Abstract from PubMedX-ray crystallography of G protein-coupled receptors and other membrane proteins is hampered by difficulties associated with growing sufficiently large crystals that withstand radiation damage and yield high-resolution data at synchrotron sources. We used an x-ray free-electron laser (XFEL) with individual 50-femtosecond-duration x-ray pulses to minimize radiation damage and obtained a high-resolution room-temperature structure of a human serotonin receptor using sub-10-micrometer microcrystals grown in a membrane mimetic matrix known as lipidic cubic phase. Compared with the structure solved by using traditional microcrystallography from cryo-cooled crystals of about two orders of magnitude larger volume, the room-temperature XFEL structure displays a distinct distribution of thermal motions and conformations of residues that likely more accurately represent the receptor structure and dynamics in a cellular environment. Serial femtosecond crystallography of G protein-coupled receptors.,Liu W, Wacker D, Gati C, Han GW, James D, Wang D, Nelson G, Weierstall U, Katritch V, Barty A, Zatsepin NA, Li D, Messerschmidt M, Boutet S, Williams GJ, Koglin JE, Seibert MM, Wang C, Shah ST, Basu S, Fromme R, Kupitz C, Rendek KN, Grotjohann I, Fromme P, Kirian RA, Beyerlein KR, White TA, Chapman HN, Caffrey M, Spence JC, Stevens RC, Cherezov V Science. 2013 Dec 20;342(6165):1521-4. doi: 10.1126/science.1244142. PMID:24357322[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Bacillus coli migula 1895
- Barty, A
- Basu, S
- Beyerlein, K R
- Boutet, S
- Caffrey, M
- Chapman, H N
- Cherezov, V
- Fromme, P
- Fromme, R
- GPCR, GPCR Network
- Gati, C
- Grotjohann, I
- Han, G W
- James, D
- Katritch, V
- Kirian, R A
- Koglin, J E
- Kupitz, C
- Li, D
- Liu, W
- Messerschmidt, M
- Nelson, G
- Rendek, K N
- Seibert, M M
- Shah, S T.A
- Spence, J C.H
- Stevens, R C
- Wacker, D
- Wang, C
- Wang, D
- Weierstall, U
- White, T A
- Williams, G J
- Zatsepin, N A
- Electron transport
- Ergotamine
- Free electron laser
- Gpcr
- Gpcr network
- Human 5ht2b receptor
- Lipidic cubic phase
- Membrane
- Membrane protein
- Novel protein engineering
- Psi-biology
- Serial femtosecond crystallography
- Signaling protein
- Structural genomic