Three-Dimensional Structure of Fab Fragment of Monoclonal Antibody LNKB-2 Complexed with Antigenic Nonaptide from Human Interleukin-2
- Authors: Goryacheva E.A.1, Artemyev I.V.1, Pletnevа N.V.1, Pletnev V.Z.1
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Affiliations:
- Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences
- Issue: Vol 49, No 3 (2023)
- Pages: 285-290
- Section: Articles
- URL: https://journals.rcsi.science/0132-3423/article/view/139151
- DOI: https://doi.org/10.31857/S0132342323010098
- EDN: https://elibrary.ru/GFDHZS
- ID: 139151
Cite item
Abstract
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.
About the authors
E. A. Goryacheva
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences
Author for correspondence.
Email: goryacheva@ibch.ru
Russia, 117997, Moscow, ul. Miklukho-Maklaya 16/10
I. V. 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. V. 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. Z. 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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