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5IML

Nanobody targeting human Vsig4 in Spacegroup P212121

5IML の概要
エントリーDOI10.2210/pdb5iml/pdb
関連するPDBエントリー5IMK 5IMM 5IMO
分子名称V-set and immunoglobulin domain-containing protein 4, Nanobody (3 entities in total)
機能のキーワードnanobody, complement receptor, vsig4 crig, immune system
由来する生物種Homo sapiens (Human)
詳細
細胞内の位置Membrane ; Single-pass type I membrane protein : Q9Y279
タンパク質・核酸の鎖数2
化学式量合計39205.79
構造登録者
Wen, Y. (登録日: 2016-03-06, 公開日: 2017-01-11, 最終更新日: 2024-10-16)
主引用文献Wen, Y.,Ouyang, Z.,Schoonooghe, S.,Luo, S.,De Baetselier, P.,Lu, W.,Muyldermans, S.,Raes, G.,Zheng, F.
Structural evaluation of a nanobody targeting complement receptor Vsig4 and its cross reactivity
Immunobiology, 222:807-813, 2017
Cited by
PubMed Abstract: Vsig4 is a recently identified immune regulatory protein related to the B7 family with dual functionality: a negative regulator of T cell activation and a receptor for the complement components C3b and C3c. Here we present a structural evaluation of a nanobody, Nb119, against the extracellular IgV domain protein of both mouse and human recombinant Vsig4, which have a high degree of sequence identity. Although mouse and human Vsig4 bind to Nb119 with a 250 times difference in dissociation constants, the interaction results in a highly identical assembly with a RMSD of 0.4Å. The molecular determinants for Vsig4 recognition and cross reactivity unveiled by the atomic structure of Nb119 in complex with mVsig4 and hVsig4 afford new insights useful for the further optimization of the nanobody for potential use in humans. Additionally, structural analysis of the Vsig4-Nb119 complexes indicates that Nb119 occupies the interface on Vsig4 recognized by the macroglobulin-like domains MG4 and MG5 of C3b. Thus an affinity-improved Nb119 may have the potential to influence the activation of both T cells and complement.
PubMed: 27889311
DOI: 10.1016/j.imbio.2016.11.008
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.8 Å)
構造検証レポート
Validation report summary of 5iml
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2026-02-11に公開中

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