PDBsum entry 1ci5

Immune system

PDB id: 1ci5

Contents

Protein chain

95 a.a. *

* Residue conservation analysis

PDB id:

1ci5

Name:

Immune system

Title:

Glycan-free mutant adhesion domain of human cd58 (lfa-3)

Structure:

Protein (lymphocyte function-associated antigen 3(cd58)). Chain: a. Fragment: adhesion domain. Synonym: 1dcd58-6m. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Cellular_location: cell surface. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

Z.Y.J.Sun,V.Dotsch,M.Kim,J.Li,E.L.Reinherz,G.Wagner

Key ref:

Z.Y.Sun et al. (1999). Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studies. EMBO J, 18, 2941-2949. PubMed id: 10357807 DOI: 10.1093/emboj/18.11.2941

Date:

07-Apr-99 Release date: 22-Jun-99

Protein chain

P19256  (LFA3_HUMAN) -  Lymphocyte function-associated antigen 3 from Homo sapiens

Seq: 250 a.a.

Struc: 95 a.a.*

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

DOI no: 10.1093/emboj/18.11.2941

EMBO J 18:2941-2949 (1999)

PubMed id: 10357807

Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studies.

Z.Y.Sun, V.Dötsch, M.Kim, J.Li, E.L.Reinherz, G.Wagner.

ABSTRACT

A general strategy is presented here for producing glycan-free forms of glycoproteins without loss of function by employing apolar-to-polar mutations of surface residues in functionally irrelevant epitopes. The success of this structure-based approach was demonstrated through the expression in Escherichia coli of a soluble 11 kDa adhesion domain extracted from the heavily glycosylated 55 kDa human CD58 ectodomain. The solution structure was subsequently determined and binding to its counter-receptor CD2 studied by NMR. This mutant adhesion domain is functional as determined by several experimental methods, and the size of its binding site has been probed by chemical shift perturbations in NMR titration experiments. The new structural information supports a 'hand-shake' model of CD2-CD58 interaction involving the GFCC'C" faces of both CD2 and CD58 adhesion domains. The region responsible for binding specificity is most likely localized on the C, C' and C" strands and the C-C' and C'-C" loops on CD58.

Selected figure(s)

Figure 2.
Figure 2 Space-filling structural models for (A) a homology model of the wild-type adhesion domain of CD58 depicting surface-exposed hydrophobic residues and (B) the NMR structure of 1dCD58[6m] depicting mutation sites. The molecules are viewed edge-on, with -strands A and B directly in the front. Proline and glycine residues are colored in yellow, other hydrophobic residues in green, mutation sites in red, and putative glycan attachment positions in blue. The graphs were prepared using GRASP (Nicholls et al., 1991).

Figure 4.
Figure 4 Ribbon diagrams of (A) 1dCD58[6m], (B) homology model of wild-type 1dCD58 and (C) NMR structure of the wild-type adhesion domain of human CD2 (Withka et al., 1993; Bodian et al., 1994; Wyss et al., 1995). The graphs were prepared using MOLSCRIPT (Kraulis, 1991).

The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (1999, 18, 2941-2949) copyright 1999.

Figures were selected by an automated process.