PDBsum entry 5imm

Immune system

PDB id: 5imm

Contents

Protein chains

125 a.a.

120 a.a.

Waters ×436

PDB id:

5imm

Name:

Immune system

Title:

Nanobody targeting mouse vsig4 in spacegroup p212121

Structure:

Nanobody. Chain: b. Engineered: yes. Protein vsig4. Chain: a. Fragment: igv domain, unp residues 19-139. Engineered: yes

Source:

Camelidae. Organism_taxid: 9835. Expressed in: escherichia coli. Expression_system_taxid: 562. Mus musculus. Mouse. Organism_taxid: 10090. Gene: vsig4.

Resolution:

1.20Å R-factor: 0.157 R-free: 0.176

Authors:

Y.Wen,F.Zheng

Key ref:

Y.Wen et al. (2017). Structural evaluation of a nanobody targeting complement receptor Vsig4 and its cross reactivity. Immunobiology, 222, 807-813. PubMed id: 27889311 DOI: 10.1016/j.imbio.2016.11.008

Date:

06-Mar-16 Release date: 11-Jan-17

Protein chain

No UniProt id for this chain

Struc: 125 a.a.

Protein chain

F6TUL9  (F6TUL9_MOUSE) -  V-set and immunoglobulin domain containing 4 from Mus musculus

Seq: 280 a.a.

Struc: 120 a.a.

DOI no: 10.1016/j.imbio.2016.11.008

Immunobiology 222:807-813 (2017)

PubMed id: 27889311

Structural evaluation of a nanobody targeting complement receptor Vsig4 and its cross reactivity.

Y.Wen, Z.Ouyang, S.Schoonooghe, S.Luo, P.De Baetselier, W.Lu, S.Muyldermans, G.Raes, F.Zheng.

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.