Article
Computational design of an integrin I domain stabilized in the open high affinity conformation.
Nature structural biology - 1 Aug 2000
Shimaoka M, Shifman J M, Jing H, Takagi J, Mayo S L, Springer T A
Abstract excerpt
We have taken a computational approach to design mutations that stabilize a large protein domain of approximately 200 residues in two alternative conformations. Mutations in the hydrophobic core of the alphaMbeta2 integrin I domain were designed to stabilize the crystallographically defined open or closed conformers. When expressed on the cell surface as part of the intact heterodimeric receptor, binding of the...
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