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5DVL

Fc Design 20.8.37 A chain homodimer Y349S/T366M/K370Y/K409V

Summary for 5DVL
Entry DOI10.2210/pdb5dvl/pdb
Related5DI8 5DJ0 5DJ2 5DJ6 5DJ8 5DJA 5DJC 5DJD 5DJX 5DJY 5DJZ 5DK0 5DK2 5DVK 5DVM 5DVN 5DVO
DescriptorIg gamma-1 chain C region, Fc-III peptide (3 entities in total)
Functional Keywordshead-to-tail homodimer, immunoglobulin, fc, immune system
Biological sourceHomo sapiens (Human)
More
Cellular locationSecreted: P01857
Total number of polymer chains2
Total formula weight27104.71
Authors
Primary citationLeaver-Fay, A.,Froning, K.J.,Atwell, S.,Aldaz, H.,Pustilnik, A.,Lu, F.,Huang, F.,Yuan, R.,Hassanali, S.,Chamberlain, A.K.,Fitchett, J.R.,Demarest, S.J.,Kuhlman, B.
Computationally Designed Bispecific Antibodies using Negative State Repertoires.
Structure, 24:641-651, 2016
Cited by
PubMed Abstract: A challenge in the structure-based design of specificity is modeling the negative states, i.e., the complexes that you do not want to form. This is a difficult problem because mutations predicted to destabilize the negative state might be accommodated by small conformational rearrangements. To overcome this challenge, we employ an iterative strategy that cycles between sequence design and protein docking in order to build up an ensemble of alternative negative state conformations for use in specificity prediction. We have applied our technique to the design of heterodimeric CH3 interfaces in the Fc region of antibodies. Combining computationally and rationally designed mutations produced unique designs with heterodimer purities greater than 90%. Asymmetric Fc crystallization was able to resolve the interface mutations; the heterodimer structures confirmed that the interfaces formed as designed. With these CH3 mutations, and those made at the heavy-/light-chain interface, we demonstrate one-step synthesis of four fully IgG-bispecific antibodies.
PubMed: 26996964
DOI: 10.1016/j.str.2016.02.013
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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