2bg9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2bg9.gif|left|200px]]<br /><applet load="2bg9" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2bg9.gif|left|200px]]
-
caption="2bg9, resolution 4.00&Aring;" />
+
 
-
'''REFINED STRUCTURE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR AT 4A RESOLUTION.'''<br />
+
{{Structure
 +
|PDB= 2bg9 |SIZE=350|CAPTION= <scene name='initialview01'>2bg9</scene>, resolution 4.00&Aring;
 +
|SITE=
 +
|LIGAND=
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''REFINED STRUCTURE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR AT 4A RESOLUTION.'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
2BG9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Torpedo_marmorata Torpedo marmorata]. The following page contains interesting information on the relation of 2BG9 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb71_1.html Acetylcholine Receptor]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BG9 OCA].
+
2BG9 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Torpedo_marmorata Torpedo marmorata]. The following page contains interesting information on the relation of 2BG9 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb71_1.html Acetylcholine Receptor]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BG9 OCA].
==Reference==
==Reference==
-
Refined structure of the nicotinic acetylcholine receptor at 4A resolution., Unwin N, J Mol Biol. 2005 Mar 4;346(4):967-89. Epub 2005 Jan 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15701510 15701510]
+
Refined structure of the nicotinic acetylcholine receptor at 4A resolution., Unwin N, J Mol Biol. 2005 Mar 4;346(4):967-89. Epub 2005 Jan 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15701510 15701510]
[[Category: Acetylcholine Receptor]]
[[Category: Acetylcholine Receptor]]
[[Category: Protein complex]]
[[Category: Protein complex]]
Line 21: Line 30:
[[Category: postsynaptic membrane]]
[[Category: postsynaptic membrane]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:31 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:01:32 2008''

Revision as of 14:01, 20 March 2008


PDB ID 2bg9

Drag the structure with the mouse to rotate
, resolution 4.00Å
Coordinates: save as pdb, mmCIF, xml



REFINED STRUCTURE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR AT 4A RESOLUTION.


Overview

We present a refined model of the membrane-associated Torpedo acetylcholine (ACh) receptor at 4A resolution. An improved experimental density map was obtained from 342 electron images of helical tubes, and the refined structure was derived to an R-factor of 36.7% (R(free) 37.9%) by standard crystallographic methods, after placing the densities corresponding to a single molecule into an artificial unit cell. The agreement between experimental and calculated phases along the helical layer-lines was used to monitor progress in the refinement and to give an independent measure of the accuracy. The atomic model allowed a detailed description of the whole receptor in the closed-channel form, including the ligand-binding and intracellular domains, which have not previously been interpreted at a chemical level. We confirm that the two ligand-binding alpha subunits have a different extended conformation from the three other subunits in the closed channel, and identify several interactions on both pairs of subunit interfaces, and within the alpha subunits, which may be responsible for their "distorted" structures. The ACh-coordinating amino acid side-chains of the alpha subunits are far apart in the closed channel, indicating that a localised rearrangement, involving closure of loops B and C around the bound ACh molecule, occurs upon activation. A comparison of the structure of the alpha subunit with that of AChBP having ligand present, suggests how the localised rearrangement overcomes the distortions and initiates the rotational movements associated with opening of the channel. Both vestibules of the channel are strongly electronegative, providing a cation-stabilising environment at either entrance of the membrane pore. Access to the pore on the intracellular side is further influenced by narrow lateral windows, which would be expected to screen out electrostatically ions of the wrong charge and size.

About this Structure

2BG9 is a Protein complex structure of sequences from Torpedo marmorata. The following page contains interesting information on the relation of 2BG9 with [Acetylcholine Receptor]. Full crystallographic information is available from OCA.

Reference

Refined structure of the nicotinic acetylcholine receptor at 4A resolution., Unwin N, J Mol Biol. 2005 Mar 4;346(4):967-89. Epub 2005 Jan 25. PMID:15701510

Page seeded by OCA on Thu Mar 20 16:01:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools