PDBsum entry 1cfq

Polyspecificity

PDB id: 1cfq

Contents

Protein chains

214 a.a. *

213 a.a. *

Waters ×30

* Residue conservation analysis

PDB id:

1cfq

Name:

Polyspecificity

Title:

Anti-p24 (HIV-1) fab fragment cb41

Structure:

Protein (igg2a kappa antibody cb41 (light chain)). Chain: a. Fragment: fab. Protein (igg2a kappa antibody cb41 (heavy chain)). Chain: b. Fragment: fab

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Strain: balb/c. Cell_line: cb 4/1/1/f6 b-cell hybridoma. Cell_line: cb 4/1/1/f6 b-cell hybridoma

Biol. unit:

Dimer (from PQS)

Resolution:

2.80Å R-factor: 0.221 R-free: 0.312

Authors:

T.Keitel,A.Kramer,H.Wessner,C.Scholz,J.Schneider-Mergener,W.Hoehne

Key ref:

T.Keitel et al. (1997). Crystallographic analysis of anti-p24 (HIV-1) monoclonal antibody cross-reactivity and polyspecificity. Cell, 91, 811-820. PubMed id: 9413990 DOI: 10.1016/S0092-8674(00)80469-9

Date:

19-Mar-99 Release date: 30-Mar-99

Protein chain

P01837  (IGKC_MOUSE) -  Immunoglobulin kappa constant from Mus musculus

Seq: 107 a.a.

Struc: 214 a.a.*

Protein chain

P01864  (GCAB_MOUSE) -  Ig gamma-2A chain C region secreted form from Mus musculus

Seq: 335 a.a.

Struc: 213 a.a.

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DOI no: 10.1016/S0092-8674(00)80469-9

Cell 91:811-820 (1997)

PubMed id: 9413990

Crystallographic analysis of anti-p24 (HIV-1) monoclonal antibody cross-reactivity and polyspecificity.

T.Keitel, A.Kramer, H.Wessner, C.Scholz, J.Schneider-Mergener, W.Höhne.

ABSTRACT

The X-ray crystal structures of an anti-p24 (HIV-1) monoclonal antibody Fab fragment alone and in complexes with the epitope peptide GATPQDLNTnL (n = norleucine), an epitope-homologous peptide GATPEDLNQKLAGN, as well as two unrelated peptides GLYEWGGARITNTD and efslkGpllqwrsG (D-peptide), are presented to a maximum resolution of 2.6 A. The latter three peptides were identified from screening synthetic combinatorial peptide libraries. Although all peptides bind to the same antigen combining site, the nonhomologous peptides adopt different binding conformations and also form their critical contacts with different antibody residues. Only small readjustments are observed within the framework of the Fab fragment upon binding.

Selected figure(s)

Figure 1.
Figure 1. Difference Electron Density Map for the h-pep/CB4-1 ComplexThe difference electron density was computed with the 2.60 Å resolution structure amplitudes from the CB4-1/h-pep crystal and with refined model phases from CB4-1. Density is shown for >3σ.

Figure 2.
Figure 2. Superposition of Variable Domains and Overlay of Complexed Peptides(A) Variable domain superposition. Residues from conserved β regions of V[L] (4–6, 20–25, 33–38, 45–48, 63–65, 70–74, 86–89, 102–104) were superimposed to visualize the V[L]/V[H] rearrangements. The Cα framework atoms are oriented with V[L] at the left. Peptides are omitted. Uncomplexed CB4-1, black; complexed with e-pep, yellow; h-pep, red; u-pep, purple; d-pep, green.(B) Peptide overlay. Superposition of V[L] and V[H] domains was performed as described in Table 2. Only the peptides are displayed: e-pep, yellow; h-pep, red; u-pep, purple; d-pep, green (N terminus: right). For a general overview of the peptides in complex with CB4-1 Fab, see Figure 4 in [27].

The above figures are reprinted by permission from Cell Press: Cell (1997, 91, 811-820) copyright 1997.