[Effect of immunoglobulin G1 Pro 290 residue on structural and biological characteristics of its SH2 domain].
Tryptic hydrolysis of only one of 11 studied Fc fragments of human myeloma immunoglobulins G1 (IgG1) provided an intact CH2 domain in a high yield (up to 40% as opposed to 2-3% for other IgG1s). The only structural difference of this domain was shown to be the substitution of Pro for Lys290. This decreased the capacity of the IgG1 Sem Fc fragment to interact with proteins of the complement system.
Tishchenko
V M
VM
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, Russia. tischen@sun.ipr.serpukhov.su
D019943:Amino Acid Substitution; D006801:Humans; D006868:Hydrolysis; D007141:Immunoglobulin Fc Fragments / Q000737:chemistry; D007074:Immunoglobulin G / Q000737:chemistry*; D008239:Lysine / Q000737:chemistry*; D009194:Myeloma Proteins / Q000737:chemistry*; D011392:Proline / Q000737:chemistry*; D018909:src Homology Domains
D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D009194:Myeloma Proteins; D011392:Proline; D008239:Lysine