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Default NMR analysis reveals a positively charged hydrophobic domain as a common motif to bou

NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine.

Related Articles NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine.

Biochemistry. 1994 Jan 25;33(3):644-50

Authors: Fraenkel Y, Gershoni JM, Navon G

A complete 1H assignment of d-tubocurarine was carried out using 1D and 2D NMR techniques. Geometries of free acetylcholine (ACh) and d-tubocurarine were compared with those of the ligands bound to a recombinant cholinergic binding site (T alpha 184-200 expressed as a fusion protein in Escherichia coli). The conformations of the free ligands were determined by NOESY experiments while those of the bound molecules were obtained by transferred NOESY. The complete relaxation matrix was solved yielding distance constraints which were further refined by a sigma back-calculation. ACh bound to recombinant T alpha 184-200 closely resembled the conformation previously reported for ACh bound to the intact receptor. d-Tubocurarine in the bound state undergoes extensive induced conformational rearrangements generating a "cup"-shaped structure. A unique positively charged hydrophobic domain is identified as characteristic of both bound cholinergic ligands.

PMID: 8292592 [PubMed - indexed for MEDLINE]



Source: PubMed
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