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1F90

FAB FRAGMENT OF MONOCLONAL ANTIBODY (LNKB-2) AGAINST HUMAN INTERLEUKIN-2 IN COMPLEX WITH ANTIGENIC PEPTIDE

1F90 の概要
エントリーDOI10.2210/pdb1f90/pdb
分子名称FAB FRAGMENT OF MONOCLONAL ANTIBODY, ANTIGENIC NONAPEPTIDE, ... (4 entities in total)
機能のキーワードmonoclonal antibody, antigen-binding fragment, interleukin-2, antigenic peptide, immune system
由来する生物種Mus musculus (house mouse)
詳細
タンパク質・核酸の鎖数3
化学式量合計49112.75
構造登録者
主引用文献Afonin, P.V.,Fokin, A.V.,Tsygannik, I.N.,Mikhailova, I.Y.,Onoprienko, L.V.,Mikhaleva, I.I.,Ivanov, V.T.,Mareeva, T.Y.,Nesmeyanov, V.A.,Li, N.,Pangborn, W.A.,Duax, W.L.,Pletnev, V.Z.
Crystal structure of an anti-interleukin-2 monoclonal antibody Fab complexed with an antigenic nonapeptide.
Protein Sci., 10:1514-1521, 2001
Cited by
PubMed Abstract: The three-dimensional structure of the Fab fragment of a monoclonal antibody (LNKB-2) to human interleukin-2 (IL-2) complexed with a synthetic antigenic nonapeptide, Ac-Lys-Pro-Leu-Glu-Glu-Val-Leu-Asn-Leu-OMe, has been determined at 3.0 A resolution. In the structure, four out of the six hypervariable loops of the Fab (complementarity determining regions [CDRs] L1, H1, H2, and H3) are involved in peptide association through hydrogen bonding, salt bridge formation, and hydrophobic interactions. The Tyr residues in the Fab antigen binding site play a major role in antigen-antibody recognition. The structures of the complexed and uncomplexed Fab were compared. In the antigen binding site the CDR-L1 loop of the antibody shows the largest structural changes upon peptide binding. The peptide adopts a mostly alpha-helical conformation similar to that in the epitope fragment 64-72 of the IL-2 antigen. The side chains of residues Leu 66, Val 69, and Leu 70, which are shielded internally in the IL-2 structure, are involved in interactions with the Fab in the complex studied. This indicates that antibody-antigen complexation involves a significant rearrangement of the epitope-containing region of the IL-2 with retention of the alpha-helical character of the epitope fragment.
PubMed: 11468348
DOI: 10.1110/ps.3101
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.6 Å)
構造検証レポート
Validation report summary of 1f90
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-24に公開中

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