6h7m: Difference between revisions

Line 1:

==ACTIVATED TURKEY BETA1 ADRENOCEPTOR WITH BOUND PARTIAL AGONIST SALBUTAMOL AND NANOBODY Nb6B9==

== Structural highlights ==

<table><tr><td colspan='2'>[[6h7m]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895], [http://en.wikipedia.org/wiki/Ecoli Ecoli] and [http://en.wikipedia.org/wiki/Melga Melga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H7M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H7M FirstGlance]. <br>

Line 10:

== Function ==

[[http://www.uniprot.org/uniprot/THIO_ECOLI THIO_ECOLI]] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. [[http://www.uniprot.org/uniprot/ADRB1_MELGA ADRB1_MELGA]] Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity.

== Publication Abstract from PubMed ==

G protein-coupled receptors (GPCRs) in the G protein-coupled active state have higher affinity for agonists compared to when they are in the inactive state, but the molecular basis for this is unclear. We have determined four active-state structures of the beta1-adrenoceptor (beta1AR) bound to conformation-specific nanobodies in the presence of agonists of varying efficacy. Comparison with inactive-state structures of beta1AR bound to the identical ligands showed a 24-42% reduction in the volume of the orthosteric binding site. Potential hydrogen bonds were also shorter, and there was up to a 30% increase in the number of atomic contacts between the receptor and ligand. This explains the increase in agonist affinity of GPCRs in the active state for a wide range of structurally distinct agonists.

Molecular basis for high-affinity agonist binding in GPCRs.,Warne T, Edwards PC, Dore AS, Leslie AGW, Tate CG Science. 2019 May 9. pii: science.aau5595. doi: 10.1126/science.aau5595. PMID:31072904<ref>PMID:31072904</ref>

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

</div>

==See Also==

*[[Adrenergic receptor 3D structures|Adrenergic receptor 3D structures]]

*[[Antibody 3D structures|Antibody 3D structures]]

== References ==

__TOC__

</StructureSection>

[[Category: Bacillus coli migula 1895]]

[[Category: Ecoli]]

[[Category: Large Structures]]

[[Category: Melga]]

[[Category: Dore, A S]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
 ==ACTIVATED TURKEY BETA1 ADRENOCEPTOR WITH BOUND PARTIAL AGONIST SALBUTAMOL AND NANOBODY Nb6B9==
-<StructureSection load='6h7m' size='340' side='right' caption='[[6h7m]], [[Resolution|resolution]] 2.76&Aring;' scene=''>
+<StructureSection load='6h7m' size='340' side='right'caption='[[6h7m]], [[Resolution|resolution]] 2.76&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[6h7m]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895], [http://en.wikipedia.org/wiki/Ecoli Ecoli] and [http://en.wikipedia.org/wiki/Melga Melga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H7M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H7M FirstGlance]. <br>
@@ Line 10: / Line 10: @@
 == Function ==
 [[http://www.uniprot.org/uniprot/THIO_ECOLI THIO_ECOLI]] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. [[http://www.uniprot.org/uniprot/ADRB1_MELGA ADRB1_MELGA]] Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+G protein-coupled receptors (GPCRs) in the G protein-coupled active state have higher affinity for agonists compared to when they are in the inactive state, but the molecular basis for this is unclear. We have determined four active-state structures of the beta1-adrenoceptor (beta1AR) bound to conformation-specific nanobodies in the presence of agonists of varying efficacy. Comparison with inactive-state structures of beta1AR bound to the identical ligands showed a 24-42% reduction in the volume of the orthosteric binding site. Potential hydrogen bonds were also shorter, and there was up to a 30% increase in the number of atomic contacts between the receptor and ligand. This explains the increase in agonist affinity of GPCRs in the active state for a wide range of structurally distinct agonists.
+Molecular basis for high-affinity agonist binding in GPCRs.,Warne T, Edwards PC, Dore AS, Leslie AGW, Tate CG Science. 2019 May 9. pii: science.aau5595. doi: 10.1126/science.aau5595. PMID:31072904<ref>PMID:31072904</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6h7m" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Adrenergic receptor 3D structures|Adrenergic receptor 3D structures]]
+*[[Antibody 3D structures|Antibody 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
 [[Category: Bacillus coli migula 1895]]
 [[Category: Ecoli]]
+[[Category: Large Structures]]
 [[Category: Melga]]
 [[Category: Dore, A S]]