4nc3: Difference between revisions

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{{STRUCTURE_4nc3|  PDB=4nc3  |  SCENE=  }}
==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]] 2.80&Aring;' scene=''>
{{ABSTRACT_PUBMED_24357322}}
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4nc3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NC3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NC3 FirstGlance]. <br>
==Function==
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=DGA:DIACYL+GLYCEROL'>DGA</scene>, <scene name='pdbligand=ERM:ERGOTAMINE'>ERM</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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='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>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/5HT2B_HUMAN 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.  
[[http://www.uniprot.org/uniprot/5HT2B_HUMAN 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.  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
X-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.


==About this Structure==
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<ref>PMID:24357322</ref>
[[4nc3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NC3 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<ref group="xtra">PMID:024357322</ref><references group="xtra"/><references/>
</div>
[[Category: Barty, A.]]
== References ==
[[Category: Basu, S.]]
<references/>
[[Category: Beyerlein, K R.]]
__TOC__
[[Category: Boutet, S.]]
</StructureSection>
[[Category: Caffrey, M.]]
[[Category: Bacillus coli migula 1895]]
[[Category: Chapman, H N.]]
[[Category: Barty, A]]
[[Category: Cherezov, V.]]
[[Category: Basu, S]]
[[Category: Fromme, P.]]
[[Category: Beyerlein, K R]]
[[Category: Fromme, R.]]
[[Category: Boutet, S]]
[[Category: GPCR, GPCR Network.]]
[[Category: Caffrey, M]]
[[Category: Gati, C.]]
[[Category: Chapman, H N]]
[[Category: Grotjohann, I.]]
[[Category: Cherezov, V]]
[[Category: Han, G W.]]
[[Category: Fromme, P]]
[[Category: James, D.]]
[[Category: Fromme, R]]
[[Category: Katritch, V.]]
[[Category: GPCR, GPCR Network]]
[[Category: Kirian, R A.]]
[[Category: Gati, C]]
[[Category: Koglin, J E.]]
[[Category: Grotjohann, I]]
[[Category: Kupitz, C.]]
[[Category: Han, G W]]
[[Category: Li, D.]]
[[Category: James, D]]
[[Category: Liu, W.]]
[[Category: Katritch, V]]
[[Category: Messerschmidt, M.]]
[[Category: Kirian, R A]]
[[Category: Nelson, G.]]
[[Category: Koglin, J E]]
[[Category: Rendek, K N.]]
[[Category: Kupitz, C]]
[[Category: Seibert, M M.]]
[[Category: Li, D]]
[[Category: Shah, S T.A.]]
[[Category: Liu, W]]
[[Category: Spence, J C.H.]]
[[Category: Messerschmidt, M]]
[[Category: Stevens, R C.]]
[[Category: Nelson, G]]
[[Category: Wacker, D.]]
[[Category: Rendek, K N]]
[[Category: Wang, C.]]
[[Category: Seibert, M M]]
[[Category: Wang, D.]]
[[Category: Shah, S T.A]]
[[Category: Weierstall, U.]]
[[Category: Spence, J C.H]]
[[Category: White, T A.]]
[[Category: Stevens, R C]]
[[Category: Williams, G J.]]
[[Category: Wacker, D]]
[[Category: Zatsepin, N A.]]
[[Category: Wang, C]]
[[Category: Wang, D]]
[[Category: Weierstall, U]]
[[Category: White, T A]]
[[Category: Williams, G J]]
[[Category: Zatsepin, N A]]
[[Category: Electron transport]]
[[Category: Electron transport]]
[[Category: Ergotamine]]
[[Category: Ergotamine]]

Revision as of 19:08, 25 December 2014

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

4nc3 is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , , , , ,
Gene:5HT2B_HUMAN, cybC ("Bacillus coli" Migula 1895)
Resources:FirstGlance, OCA, RCSB, PDBsum

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 PubMed

X-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.

References

  1. 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. Serial femtosecond crystallography of G protein-coupled receptors. Science. 2013 Dec 20;342(6165):1521-4. doi: 10.1126/science.1244142. PMID:24357322 doi:http://dx.doi.org/10.1126/science.1244142

4nc3, resolution 2.80Å

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