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1i9b

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Revision as of 09:51, 15 September 2021

X-RAY STRUCTURE OF ACETYLCHOLINE BINDING PROTEIN (ACHBP)

Structural highlights

1i9b is a 5 chain structure with sequence from Great pond snail. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ACHP_LYMST] Binds to acetylcholine. Modulates neuronal synaptic transmission.

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

Pentameric ligand gated ion-channels, or Cys-loop receptors, mediate rapid chemical transmission of signals. This superfamily of allosteric transmembrane proteins includes the nicotinic acetylcholine (nAChR), serotonin 5-HT3, gamma-aminobutyric-acid (GABAA and GABAC) and glycine receptors. Biochemical and electrophysiological information on the prototypic nAChRs is abundant but structural data at atomic resolution have been missing. Here we present the crystal structure of molluscan acetylcholine-binding protein (AChBP), a structural and functional homologue of the amino-terminal ligand-binding domain of an nAChR alpha-subunit. In the AChBP homopentamer, the protomers have an immunoglobulin-like topology. Ligand-binding sites are located at each of five subunit interfaces and contain residues contributed by biochemically determined 'loops' A to F. The subunit interfaces are highly variable within the ion-channel family, whereas the conserved residues stabilize the protomer fold. This AChBP structure is relevant for the development of drugs against, for example, Alzheimer's disease and nicotine addiction.

Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors.,Brejc K, van Dijk WJ, Klaassen RV, Schuurmans M, van Der Oost J, Smit AB, Sixma TK Nature. 2001 May 17;411(6835):269-76. PMID:11357122^[1]

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

References

↑ Brejc K, van Dijk WJ, Klaassen RV, Schuurmans M, van Der Oost J, Smit AB, Sixma TK. Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors. Nature. 2001 May 17;411(6835):269-76. PMID:11357122 doi:10.1038/35077011

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/1i9b"

@@ Line 3: / Line 3: @@
 <StructureSection load='1i9b' size='340' side='right'caption='[[1i9b]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1i9b]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Great_pond_snail Great pond snail]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I9B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I9B FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1i9b]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Great_pond_snail Great pond snail]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I9B FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></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=1i9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9b OCA], [http://pdbe.org/1i9b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i9b RCSB], [http://www.ebi.ac.uk/pdbsum/1i9b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1i9b ProSAT]</span></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=1i9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9b OCA], [https://pdbe.org/1i9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i9b RCSB], [https://www.ebi.ac.uk/pdbsum/1i9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i9b ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ACHP_LYMST ACHP_LYMST]] Binds to acetylcholine. Modulates neuronal synaptic transmission.
+[[https://www.uniprot.org/uniprot/ACHP_LYMST ACHP_LYMST]] Binds to acetylcholine. Modulates neuronal synaptic transmission.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1i9b

From Proteopedia

Revision as of 09:51, 15 September 2021

X-RAY STRUCTURE OF ACETYLCHOLINE BINDING PROTEIN (ACHBP)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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