2byn
From Proteopedia
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|PDB= 2byn |SIZE=350|CAPTION= <scene name='initialview01'>2byn</scene>, resolution 2.02Å | |PDB= 2byn |SIZE=350|CAPTION= <scene name='initialview01'>2byn</scene>, resolution 2.02Å | ||
|SITE= <scene name='pdbsite=AC1:Pg4+Binding+Site+For+Chain+E'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Pg4+Binding+Site+For+Chain+E'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2byn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2byn OCA], [http://www.ebi.ac.uk/pdbsum/2byn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2byn RCSB]</span> | ||
}} | }} | ||
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[[Category: Sulzenbacher, G.]] | [[Category: Sulzenbacher, G.]] | ||
[[Category: Taylor, P.]] | [[Category: Taylor, P.]] | ||
| - | [[Category: 1PE]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: PG4]] | ||
[[Category: acetylcholine binding protein]] | [[Category: acetylcholine binding protein]] | ||
[[Category: conformational flexibility]] | [[Category: conformational flexibility]] | ||
| Line 36: | Line 36: | ||
[[Category: soluble acetylcholine receptor]] | [[Category: soluble acetylcholine receptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:13:49 2008'' |
Revision as of 23:13, 30 March 2008
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| , resolution 2.02Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF APO ACHBP FROM APLYSIA CALIFORNICA
Overview
Upon ligand binding at the subunit interfaces, the extracellular domain of the nicotinic acetylcholine receptor undergoes conformational changes, and agonist binding allosterically triggers opening of the ion channel. The soluble acetylcholine-binding protein (AChBP) from snail has been shown to be a structural and functional surrogate of the ligand-binding domain (LBD) of the receptor. Yet, individual AChBP species display disparate affinities for nicotinic ligands. The crystal structure of AChBP from Aplysia californica in the apo form reveals a more open loop C and distinctive positions for other surface loops, compared with previous structures. Analysis of Aplysia AChBP complexes with nicotinic ligands shows that loop C, which does not significantly change conformation upon binding of the antagonist, methyllycaconitine, further opens to accommodate the peptidic antagonist, alpha-conotoxin ImI, but wraps around the agonists lobeline and epibatidine. The structures also reveal extended and nonoverlapping interaction surfaces for the two antagonists, outside the binding loci for agonists. This comprehensive set of structures reflects a dynamic template for delineating further conformational changes of the LBD of the nicotinic receptor.
About this Structure
2BYN is a Single protein structure of sequence from Aplysia californica. Full crystallographic information is available from OCA.
Reference
Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations., Hansen SB, Sulzenbacher G, Huxford T, Marchot P, Taylor P, Bourne Y, EMBO J. 2005 Oct 19;24(20):3635-46. Epub 2005 Sep 29. PMID:16193063
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