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pubmed-article:22021856pubmed:abstractTextThe manipulation of protein backbone structure to control interaction and function is a challenge for protein engineering. We integrated computational design with experimental selection for grafting the backbone and side chains of a two-segment HIV gp120 epitope, targeted by the cross-neutralizing antibody b12, onto an unrelated scaffold protein. The final scaffolds bound b12 with high specificity and with affinity similar to that of gp120, and crystallographic analysis of a scaffold bound to b12 revealed high structural mimicry of the gp120-b12 complex structure. The method can be generalized to design other functional proteins through backbone grafting.lld:pubmed
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pubmed-article:22021856pubmed:articleTitleComputation-guided backbone grafting of a discontinuous motif onto a protein scaffold.lld:pubmed
pubmed-article:22021856pubmed:affiliationDepartment of Biochemistry, University of Washington, Seattle, WA 98195, USA.lld:pubmed
pubmed-article:22021856pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:22021856pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed