Molecular Symmetry as an Aid to Geometry Determination in Ligand Protein Complexes

Dipole–dipole couplings between pairs of spin 12 nuclei, which can be measured from NMR spectra in field-ordered media, offer useful constraints on the orientation of various fragments in molecular systems. However, the orientation of fragments relative to a molecule fixed reference frame is often k...

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Bibliographic Details
Published in:Journal of magnetic resonance (1997) 2000-01, Vol.142 (1), p.153-158
Main Authors: Al-Hashimi, H.M, Bolon, P.J, Prestegard, J.H
Format: Article
Language:English
Subjects:
Carrier Proteins - chemistry
Collectins
homomultimer
Lectins - chemistry
ligand bound geometry
Magnetic Resonance Spectroscopy - methods
mannose binding protein
Methylmannosides - chemistry
order tensors
Protein Binding
symmetry
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Summary:Dipole–dipole couplings between pairs of spin 12 nuclei, which can be measured from NMR spectra in field-ordered media, offer useful constraints on the orientation of various fragments in molecular systems. However, the orientation of fragments relative to a molecule fixed reference frame is often key to complete structure determination. Here, we demonstrate that the symmetry properties of molecular complexes can aid in the definition of a reference frame. It is shown that a threefold rotational symmetry axis dictates the direction and symmetry of the experimentally determined order tensor for α-methyl-mannose in fast exchange among the three symmetry-related binding sites of mannose binding protein. This approach facilitates studies of the geometry of the ligand in the protein–ligand complex and also may provide a novel route to structure determination of a homomultimeric protein.
ISSN:1090-7807
1096-0856
DOI:10.1006/jmre.1999.1937