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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/IGKC_HUMAN IGKC_HUMAN] | [https://www.uniprot.org/uniprot/IGKC_HUMAN IGKC_HUMAN] | ||
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== Publication Abstract from PubMed == | |||
The 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. | |||
Computation-guided backbone grafting of a discontinuous motif onto a protein scaffold.,Azoitei ML, Correia BE, Ban YE, Carrico C, Kalyuzhniy O, Chen L, Schroeter A, Huang PS, McLellan JS, Kwong PD, Baker D, Strong RK, Schief WR Science. 2011 Oct 21;334(6054):373-6. PMID:22021856<ref>PMID:22021856</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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==See Also== | ==See Also== | ||
Latest revision as of 13:24, 6 November 2024
Structure of an HIV epitope scaffold in complex with neutralizing antibody b12 FabStructure of an HIV epitope scaffold in complex with neutralizing antibody b12 Fab
Structural highlights
DiseaseIGKC_HUMAN Defects in IGKC are the cause of immunoglobulin kappa light chain deficiency (IGKCD) [MIM:614102. IGKCD is a disease characterized by the complete absence of immunoglobulin kappa chains.[1] FunctionPublication Abstract from PubMedThe 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. Computation-guided backbone grafting of a discontinuous motif onto a protein scaffold.,Azoitei ML, Correia BE, Ban YE, Carrico C, Kalyuzhniy O, Chen L, Schroeter A, Huang PS, McLellan JS, Kwong PD, Baker D, Strong RK, Schief WR Science. 2011 Oct 21;334(6054):373-6. PMID:22021856[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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