3OG6

The crystal structure of human interferon lambda 1 complexed with its high affinity receptor in space group P212121

3OG6 の概要

• エントリーDOI: 10.2210/pdb3og6/pdb
• 関連するPDBエントリー: 3G9V 3HHC 3OG4
• 分子名称: Interleukin-29, Interleukin 28 receptor, alpha (Interferon, lambda receptor), beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: helical bundle, fibronectin type iii domain, beta-sandwich, cytokine signaling, membrane, cytokine-cytokine receptor complex, cytokine/cytokine receptor
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48718.15

構造登録者

Miknis, Z.J.,Magracheva, E.,Lei, W.,Zdanov, A.,Kotenko, S.V.,Wlodawer, A. (登録日: 2010-08-16, 公開日: 2010-10-20, 最終更新日: 2024-10-16)

主引用文献

Miknis, Z.J.,Magracheva, E.,Li, W.,Zdanov, A.,Kotenko, S.V.,Wlodawer, A.
Crystal structure of the complex of human interferon-lambda1 with its high affinity receptor interferon-lambdaR1.
J.Mol.Biol., 404:650-664, 2010

PubMed Abstract: Interferon (IFN)-λ1 [also known as interleukin (IL)-29] belongs to the recently discovered group of type III IFNs. All type III IFNs initiate signaling processes through formation of specific heterodimeric receptor complexes consisting of IFN-λR1 and IL-10R2. We have determined the structure of human IFN-λ1 complexed with human IFN-λR1, a receptor unique to type III IFNs. The overall structure of IFN-λ1 is topologically similar to the structure of IL-10 and other members of the IL-10 family of cytokines. IFN-λR1 consists of two distinct domains having fibronectin type III topology. The ligand-receptor interface includes helix A, loop AB, and helix F on the IFN site, as well as loops primarily from the N-terminal domain and inter-domain hinge region of IFN-λR1. Composition and architecture of the interface that includes only a few direct hydrogen bonds support an idea that long-range ionic interactions between ligand and receptor govern the process of initial recognition of the molecules while hydrophobic interactions finalize it.

PubMed: 20934432
DOI: 10.1016/j.jmb.2010.09.068

実験手法

X-RAY DIFFRACTION (2.097 Å)