3d4s

From Proteopedia

(Difference between revisions)

Revision as of 12:40, 30 August 2023

Cholesterol bound form of human beta2 adrenergic receptor.

Structural highlights

3d4s is a 1 chain structure with sequence from Escherichia virus T4 and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.8Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.ENLYS_BPT4 Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.^[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 PubMed

The role of cholesterol in eukaryotic membrane protein function has been attributed primarily to an influence on membrane fluidity and curvature. We present the 2.8 A resolution crystal structure of a thermally stabilized human beta(2)-adrenergic receptor bound to cholesterol and the partial inverse agonist timolol. The receptors pack as monomers in an antiparallel association with two distinct cholesterol molecules bound per receptor, but not in the packing interface, thereby indicating a structurally relevant cholesterol-binding site between helices I, II, III, and IV. Thermal stability analysis using isothermal denaturation confirms that a cholesterol analog significantly enhances the stability of the receptor. A consensus motif is defined that predicts cholesterol binding for 44% of human class A receptors, suggesting that specific sterol binding is important to the structure and stability of other G protein-coupled receptors, and that this site may provide a target for therapeutic discovery.

A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor.,Hanson MA, Cherezov V, Griffith MT, Roth CB, Jaakola VP, Chien EY, Velasquez J, Kuhn P, Stevens RC Structure. 2008 Jun;16(6):897-905. PMID:18547522^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Moussa SH, Kuznetsov V, Tran TA, Sacchettini JC, Young R. Protein determinants of phage T4 lysis inhibition. Protein Sci. 2012 Apr;21(4):571-82. doi: 10.1002/pro.2042. Epub 2012 Mar 2. PMID:22389108 doi:http://dx.doi.org/10.1002/pro.2042
↑ Hanson MA, Cherezov V, Griffith MT, Roth CB, Jaakola VP, Chien EY, Velasquez J, Kuhn P, Stevens RC. A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor. Structure. 2008 Jun;16(6):897-905. PMID:18547522 doi:10.1016/j.str.2008.05.001

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3d4s"

@@ Line 3: / Line 3: @@
 <StructureSection load='3d4s' size='340' side='right'caption='[[3d4s]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3d4s]] is a 1 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=3D4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D4S FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3d4s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D4S FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=TIM:(2S)-1-(TERT-BUTYLAMINO)-3-[(4-MORPHOLIN-4-YL-1,2,5-THIADIAZOL-3-YL)OXY]PROPAN-2-OL'>TIM</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2rh1|2rh1]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=TIM:(2S)-1-(TERT-BUTYLAMINO)-3-[(4-MORPHOLIN-4-YL-1,2,5-THIADIAZOL-3-YL)OXY]PROPAN-2-OL'>TIM</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADRB2, ADRB2R, B2AR / E ([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'>[https://proteopedia.org/fgij/fg.htm?mol=3d4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d4s OCA], [https://pdbe.org/3d4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d4s RCSB], [https://www.ebi.ac.uk/pdbsum/3d4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d4s ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://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.
+[https://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.[https://www.uniprot.org/uniprot/ENLYS_BPT4 ENLYS_BPT4] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.<ref>PMID:22389108</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 38: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Escherichia virus T4]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: ATCG3D, Accelerated Technologies Center for Gene to 3D Structure]]
+[[Category: Cherezov V]]
-[[Category: Cherezov, V]]
+[[Category: Chien EYT]]
-[[Category: Chien, E Y.T]]
+[[Category: Griffith MT]]
-[[Category: GPCR, GPCR Network]]
+[[Category: Hanson MA]]
-[[Category: Griffith, M T]]
+[[Category: Jaakola V-P]]
-[[Category: Hanson, M A]]
+[[Category: Kuhn P]]
-[[Category: Jaakola, V P]]
+[[Category: Roth CB]]
-[[Category: Kuhn, P]]
+[[Category: Stevens RC]]
-[[Category: Roth, C B]]
+[[Category: Velasquez J]]
-[[Category: Stevens, R C]]
-[[Category: Velasquez, J]]
-[[Category: Accelerated technologies center for gene to 3d structure]]
-[[Category: Adrenergic]]
-[[Category: Atcg3d]]
-[[Category: Fusion]]
-[[Category: G-protein coupled receptor]]
-[[Category: Glycoprotein]]
-[[Category: Gpcr]]
-[[Category: Gpcr network]]
-[[Category: Lipoprotein]]
-[[Category: Lysozyme]]
-[[Category: Membrane protein]]
-[[Category: Palmitate]]
-[[Category: Phosphoprotein]]
-[[Category: PSI, Protein structure initiative]]
-[[Category: Receptor]]
-[[Category: Structural genomic]]
-[[Category: Timolol]]
-[[Category: Transducer]]
-[[Category: Transmembrane]]

3d4s

From Proteopedia

Revision as of 12:40, 30 August 2023

Cholesterol bound form of human beta2 adrenergic receptor.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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