Framework residue 71 is a major determinant of the position and conformation of the second hypervariable region in the VH domains of immunoglobulins.
By Anna Tramontano, C. Chothia, Arthur M. Lesk. 1990
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Citations in the corpus
- SWISS-MODEL: homology modelling of protein structures and complexes (2018, neutral): “If a matching sequence signal is detected, data can be sent to the Prediction of Immunoglobulin Structure server PIGSPro (44–46) where the model of the antibody is generated according to the canonical structure method (47–49).”
- Antibody Structure and Function: The Basis for Engineering Therapeutics (2019, background): “To reduce the cross-reaction with these analogs, a phage library randomizing five antigen-binding positions in CDR-H2 and CDR L3 was constructed.”
- Exploiting evolutionary relationships for predicting protein structures (2003, background): “…family-specific loops, such as antibody hypervariable loops (Al-Lazikani et al., 1997; Chothia and Lesk, 1987; Chothia et al., 1989; Morea et al., 1997, 1998b; Tramontano et al., 1990; Tramontano and Lesk, 1992), have been demonstrated to assume main-chain structures predictable from the sequence.”
- Blind prediction performance of RosettaAntibody 3.0: Grafting, relaxation, kinematic loop modeling, and full CDR optimization (2014, background): “The structural determinants of the canonical CDR conformations includes some residues in the FRs,15,26 and the identity of these residues has a species dependence.”
- Structural Bioinformatics (unknown): “…these loops (the light chains loops and the H1 and H2 loops of the heavy chain) can only assume a limited number of conformations and that these are determined by the presence of key residues in specific positions in the sequence of the antibody (Chothia and Lesk, 1987; Tramontano et al., 1990).”
- A new clustering of antibody CDR loop conformations (2010, unknown): “1” 1GGIH(15) 1GGCH(18) H2-1 3 H2-9-1 7FABH 1GIGH 1VFAB(5) H2-2A 4 H2-10-1 1FVCD 1FGVH 1MFAH(10) 1TETH(19)”