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''' | ==In meso X-ray crystallography structure of the Beta2-adrenergic receptor at 100 K== | ||
<StructureSection load='5d5b' size='340' side='right' caption='[[5d5b]], [[Resolution|resolution]] 3.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5d5b]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D5B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D5B FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACM:ACETAMIDE'>ACM</scene>, <scene name='pdbligand=BU1:1,4-BUTANEDIOL'>BU1</scene>, <scene name='pdbligand=CAU:(2S)-1-(9H-CARBAZOL-4-YLOXY)-3-(ISOPROPYLAMINO)PROPAN-2-OL'>CAU</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=N9S:4-O-ALPHA-D-GLUCOPYRANOSYL-BETA-D-GLUCOPYRANOSE'>N9S</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </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=5d5b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d5b OCA], [http://pdbe.org/5d5b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d5b RCSB], [http://www.ebi.ac.uk/pdbsum/5d5b PDBsum]</span></td></tr> | |||
[[Category: | </table> | ||
[[Category: Huang, C | == Function == | ||
[[http://www.uniprot.org/uniprot/ADRB2_HUMAN ADRB2_HUMAN]] Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine. | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Lysozyme]] | |||
[[Category: Caffrey, M]] | |||
[[Category: Huang, C Y]] | |||
[[Category: Kobilka, B]] | |||
[[Category: Liu, X]] | |||
[[Category: Olieric, V]] | |||
[[Category: Wang, M]] | |||
[[Category: Hydrolase]] | |||
[[Category: Membrane protein]] | |||
[[Category: Membrane protein-hydrolase complex]] | |||
Revision as of 23:31, 13 January 2016
In meso X-ray crystallography structure of the Beta2-adrenergic receptor at 100 KIn meso X-ray crystallography structure of the Beta2-adrenergic receptor at 100 K
Structural highlights
Function[ADRB2_HUMAN] Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine. |
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