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Structure paper

TitleCreating an alpha-7 nicotinic acetylcholine recognition domain from the acetylcholine binding protein: crystallographic and ligand selectivity analyses
Journal, issue, pagesJ. Biol. Chem., Vol. 286, Page 42555-42565, Year 2011
Publish dateJun 15, 2011 (structure data deposition date)
AuthorsNemecz, A. / Taylor, P.
External linksJ. Biol. Chem. / PubMed:22009746
MethodsX-ray diffraction
Resolution2.32 - 3 Å
Structure data

PDB-3sh1:
Ac-AChBP ligand binding domain mutated to human alpha-7 nAChR
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-3sio:
Ac-AChBP ligand binding domain (not including beta 9-10 linker) mutated to human alpha-7 nAChR
Method: X-RAY DIFFRACTION / Resolution: 2.32 Å

PDB-3t4m:
Ac-AChBP ligand binding domain mutated to human alpha-7 nAChR (intermediate)
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-MLK:
METHYLLYCACONITINE / alkaloid*YM

ChemComp-MRD:
(4R)-2-METHYLPENTANE-2,4-DIOL / precipitant*YM

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-CA:
Unknown entry

Source
  • aplysia californica (California sea hare)
KeywordsRECEPTOR / Human nicotinic acetylcholine receptor binding protein / Methyllycaconitine Binding / Glycosylation / Mutated Acetylcholine Binding Protein / Aplysia californica / alpha-7 human nicotinic acetylcholine receptor / AChBP / nAChR / Binding Protein / Acetylcholine / Methyllycaconitine

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