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3mra

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Revision as of 06:39, 26 October 2022

M3 TRANSMEMBRANE SEGMENT OF ALPHA-SUBUNIT OF NICOTINIC ACETYLCHOLINE RECEPTOR FROM TORPEDO CALIFORNICA, NMR, 15 STRUCTURES

Structural highlights

3mra is a 1 chain structure with sequence from Tetronarce californica. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACHA_TETCF After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.

Publication Abstract from PubMed

The three-dimensional structure of a synthetic peptide corresponding to the putative transmembrane segment M3 (amino acid residues 277-301) of the alpha subunit of the nicotinic acetylcholine receptor from Torpedo californica has been studied by means of two-dimensional 1H-NMR spectroscopy in a chloroform/methanol (1:1) mixture containing 0.1 M LiClO4. Complete resonance assignment has been performed using double-quantum-filtered COSY (DQF-COSY), TOCSY and NOESY spectra. The spatial structure has been calculated using the Diana program on the basis of integrated intensities of NOESY spectra. HN-C(alpha)H and HC(alpha)-C(beta)H spin-spin coupling constants. Residues 279-297 of M3 form a right-handed helix (root mean square deviation is 0.032 nm for backbone atoms and 0.088 nm for all heavy atoms). The conformations of the 17 side chains have been unambiguously determined. The obtained structure is in accord with the photolabeling pattern of the membrane nicotinic acetylcholine receptor (nAChR) which suggests alpha-helical structure of M3 in the labeled portion [Blanton, M. P. & Cohen, J. B. (1994) Biochemistry 33, 2859-2872].

Spatial structure of the M3 transmembrane segment of the nicotinic acetylcholine receptor alpha subunit.,Lugovskoy AA, Maslennikov IV, Utkin YN, Tsetlin VI, Cohen JB, Arseniev AS Eur J Biochem. 1998 Jul 15;255(2):455-61. PMID:9716388^[1]

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

References

↑ Lugovskoy AA, Maslennikov IV, Utkin YN, Tsetlin VI, Cohen JB, Arseniev AS. Spatial structure of the M3 transmembrane segment of the nicotinic acetylcholine receptor alpha subunit. Eur J Biochem. 1998 Jul 15;255(2):455-61. PMID:9716388

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==M3 TRANSMEMBRANE SEGMENT OF ALPHA-SUBUNIT OF NICOTINIC ACETYLCHOLINE RECEPTOR FROM TORPEDO CALIFORNICA, NMR, 15 STRUCTURES==
-<StructureSection load='3mra' size='340' side='right'caption='[[3mra]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
+<StructureSection load='3mra' size='340' side='right'caption='[[3mra]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3mra]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MRA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3MRA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3mra]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetronarce_californica Tetronarce californica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MRA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MRA FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3mra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mra OCA], [http://pdbe.org/3mra PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mra RCSB], [http://www.ebi.ac.uk/pdbsum/3mra PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mra ProSAT]</span></td></tr>
+</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=3mra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mra OCA], [https://pdbe.org/3mra PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mra RCSB], [https://www.ebi.ac.uk/pdbsum/3mra PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mra ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ACHA_TETCF ACHA_TETCF]] After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
+[https://www.uniprot.org/uniprot/ACHA_TETCF ACHA_TETCF] After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 25: / Line 25: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Arseniev, A S]]
+[[Category: Tetronarce californica]]
-[[Category: Cohen, J B]]
+[[Category: Arseniev AS]]
-[[Category: Lugovskoy, A A]]
+[[Category: Cohen JB]]
-[[Category: Maslennikov, I V]]
+[[Category: Lugovskoy AA]]
-[[Category: Tsetlin, V I]]
+[[Category: Maslennikov IV]]
-[[Category: Utkin, Y N]]
+[[Category: Tsetlin VI]]
-[[Category: Alpha-helix]]
+[[Category: Utkin YN]]
-[[Category: Ion-channel]]
-[[Category: Membrane protein]]
-[[Category: Receptor]]
-[[Category: Transmembrane segment]]
-[[Category: Transmembrane segment m3 of nachr]]

3mra

From Proteopedia

Revision as of 06:39, 26 October 2022

M3 TRANSMEMBRANE SEGMENT OF ALPHA-SUBUNIT OF NICOTINIC ACETYLCHOLINE RECEPTOR FROM TORPEDO CALIFORNICA, NMR, 15 STRUCTURES

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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