Surface of the Collagen binding domain.The surface is cyan, with purple texturing on the portion that interacts with the collagen triple-helix, shown as yellow tubes. Key residues are labelled.
J. Symersky, J.M. Patti, M. Carson, M. Teale, D. Moore, L. Jin, L.J. DeLucas, M. Hook and S.V.L. Narayana (1997). (accepted by Nature Struc. Biol.)
In a collaboration with Magnus Hook's group in Houston, Narayana and Jindra Symersky have solved the X-ray structure of the ~150 residue domain by MIR methods. I've modeled the binding of model collagen, and the results have been confirmed by site-directed mutagenesis studies. The figures show the clear groove and the concave surface used to bind collagen.
Surface of the Collagen binding domain.
The surface is cyan, with purple texturing on the portion that interacts
with the collagen triple-helix, shown as yellow tubes. Key residues are
labelled.
Concave binding groove.
The view looks down the axis of the orange collagen triple-helix, shown
as tubes. The collagen-binding domain is shown as a ribbon, with key residues
involved in the binding rendered as balls-&-sticks.