scholarly journals Construction, characterization and crystal structure of a fluorescent single-chain Fv chimera

2021 ◽  
Author(s):  
Nileena Velappan
Keyword(s):  
Crystal Structure ◽  
Single Chain ◽  
Single Chain Fv

scholarly journals Crystal Structure of Anti-polysialic Acid Antibody Single Chain Fv Fragment Complexed with Octasialic Acid

2013 ◽  
Vol 288 (47) ◽  
pp. 33784-33796 ◽  
Author(s):  
Masamichi Nagae ◽  
Akemi Ikeda ◽  
Masaya Hane ◽  
Shinya Hanashima ◽  
Ken Kitajima ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Polysialic Acid ◽  
Single Chain ◽  
Single Chain Fv ◽  
Single Chain Fv Fragment

scholarly journals Crystal structure of the anti-(carcinoembryonic antigen) single-chain Fv antibody MFE-23 and a model for antigen binding based on intermolecular contacts

2000 ◽  
Vol 346 (2) ◽  
pp. 519-528 ◽  
Author(s):  
Mark K. BOEHM ◽  
Adam L. CORPER ◽  
Tommy WAN ◽  
Maninder K. SOHI ◽  
Brian J. SUTTON ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Carcinoembryonic Antigen ◽  
High Surface ◽  
Immunoglobulin Superfamily ◽  
Antigen Binding ◽  
Single Chain ◽  
Antibody Molecule ◽  
Single Chain Fv ◽  
Fv Antibody ◽  
Single Chain Fv Antibody

MFE-23 is the first single-chain Fv antibody molecule to be used in patients and is used to target colorectal cancer through its high affinity for carcinoembryonic antigen (CEA), a cell-surface member of the immunoglobulin superfamily. MFE-23 contains an N-terminal variable heavy-chain domain joined by a (Gly4Ser)3 linker to a variable light-chain (VL) domain (ĸ chain) with an 11-residue C-terminal Myc-tag. Its crystal structure was determined at 2.4 Å resolution by molecular replacement with an Rcryst of 19.0%. Five of the six antigen-binding loops, L1, L2, L3, H1 and H2, conformed to known canonical structures. The sixth loop, H3, displayed a unique structure, with a β-hairpin loop and a bifurcated apex characterized by a buried Thr residue. In the crystal lattice, two MFE-23 molecules were associated back-to-back in a manner not seen before. The antigen-binding site displayed a large acidic region located mainly within the H2 loop and a large hydrophobic region within the H3 loop. Even though this structure is unliganded within the crystal, there is an unusually large region of contact between the H1, H2 and H3 loops and the β-sheet of the VL domain of an adjacent molecule (strands DEBA) as a result of intermolecular packing. These interactions exhibited remarkably high surface and electrostatic complementarity. Of seven MFE-23 residues predicted to make contact with antigen, five participated in these lattice contacts, and this model for antigen binding is consistent with previously reported site-specific mutagenesis of MFE-23 and its effect on CEA binding.

Probing the Interaction between a High-Affinity Single-Chain Fv and a Pyrimidine (6-4) Pyrimidone Photodimer by Site-Directed Mutagenesis†

Biochemistry ◽  
1999 ◽  
Vol 38 (2) ◽  
pp. 532-539 ◽  
Author(s):  
Hiroyuki Kobayashi ◽  
Hiroshi Morioka ◽  
Kunihiro Tobisawa ◽  
Takuya Torizawa ◽  
Koichi Kato ◽  
...  
Keyword(s):  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Single Chain ◽  
High Affinity ◽  
Single Chain Fv
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