PDBsum entry 1n4x

Immune system

PDB id: 1n4x

Contents

Protein chains

113 a.a. *

120 a.a. *

Metals

_CL ×2

Waters ×530

* Residue conservation analysis

PDB id:

1n4x

Name:

Immune system

Title:

Structure of scfv 1696 at acidic ph

Structure:

Immunoglobulin kappa chain variable region. Chain: l, m. Synonym: scfv 1696 molecule 1, monoclonal antibody 1696. Engineered: yes. Immunoglobulin heavy chain variable region. Chain: h, i. Synonym: scfv 1696 molecule 2, monoclonal antibody 1696. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562

Biol. unit:

Dimer (from PQS)

Resolution:

1.70Å R-factor: 0.227 R-free: 0.256

Authors:

J.Lescar,J.Brynda,M.Fabry,M.Horejsi,P.Rezacova,J.Sedlacek,G.A.Bentley

Key ref:

J.Lescar et al. (2003). Structure of a single-chain Fv fragment of an antibody that inhibits the HIV-1 and HIV-2 proteases. Acta Crystallogr D Biol Crystallogr, 59, 955-957. PubMed id: 12777823 DOI: 10.1107/S0907444903003597

Date:

02-Nov-02 Release date: 10-Jun-03

Protein chains

P01631  (KV2A7_MOUSE) -  Ig kappa chain V-II region 26-10 from Mus musculus

Seq: 113 a.a.

Struc: 113 a.a.*

Protein chains

Q921A6  (Q921A6_MOUSE) -  Anti-CEA 79 single chain Fv (Fragment) from Mus musculus

Seq: 241 a.a.

Struc: 120 a.a.*

* PDB and UniProt seqs differ at 42 residue positions (black crosses)

DOI no: 10.1107/S0907444903003597

Acta Crystallogr D Biol Crystallogr 59:955-957 (2003)

PubMed id: 12777823

Structure of a single-chain Fv fragment of an antibody that inhibits the HIV-1 and HIV-2 proteases.

J.Lescar, J.Brynda, M.Fabry, M.Horejsi, P.Rezacova, J.Sedlacek, G.A.Bentley.

ABSTRACT

The monoclonal antibody 1696, which was raised against the HIV-1 protease, inhibits the catalytic activity of the enzyme from both the HIV-1 and HIV-2 strains. The antibody cross-reacts with peptides containing the N-terminus of the enzyme, which is highly conserved between these strains. The crystal structure of a single-chain Fv fragment of 1696 (scFv-1696) in the non-complexed form, solved at 1.7 A resolution, is compared with the previously reported non-complexed Fab-1696 and antigen-bound scFv-1696 structures. Large conformational changes in the third hypervariable region of the heavy chain and differences in relative orientation of the variable domains are observed between the different structures.

Selected figure(s)

Figure 2.
Figure 2 Comparison of the variable domains of non-complexed Fab-1696 (PDB code [59]1cl7 , blue), molecule 1 of the non-complexed scFv-1696 (this work, yellow) and complexed scFv-1696 (PDB code [60]1jp5 , red). The peptide is shown in green. Superposition has been made by optimizing the correspondence between the main-chain atoms of the V[L] domains of the three structures. Fv1696 is shown from the side of (a) and from above (b) the antigen-bindng site. The V[L] domain is shown on the left of the Fv fragment, while the V[H] domain is on the right. The third CDR of V[H] (H3) is indicated.

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2003, 59, 955-957) copyright 2003.

Figure was selected by an automated process.