4bvn

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'''Unreleased structure'''
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{{STRUCTURE_4bvn| PDB=4bvn | SCENE= }}
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===Ultra-thermostable beta1-adrenoceptor with cyanopindolol bound===
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{{ABSTRACT_PUBMED_24663151}}
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The entry 4bvn is ON HOLD until Paper Publication
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==Function==
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[[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.
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Authors: Miller, J., Nehme, R., Warne, T., Edwards, P.C., Leslie, A.G.W., Schertler, G., Tate, C.G.
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==About this Structure==
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[[4bvn]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BVN OCA].
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Description: Ultra-thermostable beta1-adrenoceptor with cyanopindolol bound
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==Reference==
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<ref group="xtra">PMID:024663151</ref><references group="xtra"/><references/>
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[[Category: Edwards, P C.]]
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[[Category: Leslie, A G.W.]]
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[[Category: Miller, J.]]
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[[Category: Nehme, R.]]
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[[Category: Schertler, G.]]
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[[Category: Tate, C G.]]
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[[Category: Warne, T.]]
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[[Category: Signaling protein]]

Revision as of 09:15, 2 April 2014

Template:STRUCTURE 4bvn

Contents

Ultra-thermostable beta1-adrenoceptor with cyanopindolol bound

Template:ABSTRACT PUBMED 24663151

Function

[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.

About this Structure

4bvn is a 1 chain structure. Full crystallographic information is available from OCA.

Reference

  • Miller-Gallacher JL, Nehme R, Warne T, Edwards PC, Schertler GF, Leslie AG, Tate CG. The 2.1 A Resolution Structure of Cyanopindolol-Bound beta1-Adrenoceptor Identifies an Intramembrane Na+ Ion that Stabilises the Ligand-Free Receptor. PLoS One. 2014 Mar 24;9(3):e92727. doi: 10.1371/journal.pone.0092727. eCollection, 2014. PMID:24663151 doi:http://dx.doi.org/10.1371/journal.pone.0092727

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OCA

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