Three-Dimensional Structure of Fab Fragment of Monoclonal Antibody LNKB-2 Complexed with Antigenic Nonaptide from Human Interleukin-2

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The three-dimensional structure of the antigen-binding fragment (Fab) of the monoclonal antibody LNKB-2 in complex with the synthetic antigenic nonapeptide of human interleukin-2 (IL-2; Lys-Pro-Leu-Glu-Glu-Val-Leu-Asn-Leu-O) was determined by X-ray method at a resolution of 2.6 Å in crystal space group P212121. The peptide adopts a somewhat distorted α-helical conformation, close to that of fragment 64–72 of the IL-2 antigen. Four out of the six hypervariable loops in the antigen-binding site of the Fab fragment are involved in nonapeptide association through hydrogen bonding, salt bridge formation, and hydrophobic interactions. Moreover, Tyr residues of an antibody play an important role in antigen-antibody recognition.

作者简介

E. Goryacheva

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences

编辑信件的主要联系方式.
Email: goryacheva@ibch.ru
Russia, 117997, Moscow, ul. Miklukho-Maklaya 16/10

I. Artemyev

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences

Email: goryacheva@ibch.ru
Russia, 117997, Moscow, ul. Miklukho-Maklaya 16/10

N. Pletnevа

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences

Email: goryacheva@ibch.ru
Russia, 117997, Moscow, ul. Miklukho-Maklaya 16/10

V. Pletnev

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences

Email: goryacheva@ibch.ru
Russia, 117997, Moscow, ul. Miklukho-Maklaya 16/10

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版权所有 © Е.А. Горячева, И.В. Артемьев, Н.В. Плетнева, В.З. Плетнев, 2023

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