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Comment
. 2003 Oct 28;100(22):12529-30.
doi: 10.1073/pnas.2335923100. Epub 2003 Oct 20.

The energetics of structural change in maltose-binding protein

David E Wemmer  1
Affiliations
Comment

The energetics of structural change in maltose-binding protein

David E Wemmer. Proc Natl Acad Sci U S A. .
No abstract available

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Figures

Fig. 1.
Fig. 1.
Structures of the open (blue, Protein Database ID code 1OMP) and closed (green, Protein Database ID code 1ANF) forms of MBP (with bound maltose in red) are shown. (Left) The lower domain was superimposed, and a line was drawn through a helix in the open form, with another drawn through the same helix of the closed form, rotating the line by 35°. (Center and Right) The open (Center) and closed (Right) forms are shown separately. Blue arrowheads show general regions of contact with the receptor, which are closely space in the closed form but well separated in the open state. Red arrowheads indicate the region in which packing is altered as the protein closes. The sites at which mutations that affect opening were identified are indicated in yellow.
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