PDBsum entry 1k7b

Membrane protein

PDB id: 1k7b

Contents

Protein chain

42 a.a. *

* Residue conservation analysis

PDB id:

1k7b

Name:

Membrane protein

Title:

Nmr solution structure of stva47, the viral-binding domain of tva

Structure:

Subgroup a rous sarcoma virus receptor pg800 and pg950. Chain: a. Fragment: soluble extracellular viral-binding domain. Synonym: low density lipoprotein receptor-related protein. Engineered: yes

Source:

Coturnix coturnix. Common quail. Organism_taxid: 9091. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

M.Tonelli,R.J.Peters,T.L.James,D.A.Agard

Key ref:

M.Tonelli et al. (2001). The solution structure of the viral binding domain of Tva, the cellular receptor for subgroup A avian leukosis and sarcoma virus. FEBS Lett, 509, 161-168. PubMed id: 11768384 DOI: 10.1016/S0014-5793(01)03086-1

Date:

18-Oct-01 Release date: 19-Dec-01

Protein chain

P98162  (RSVR_COTJA) -  Subgroup A Rous sarcoma virus receptor pg950 from Coturnix japonica

Seq: 157 a.a.

Struc: 42 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1016/S0014-5793(01)03086-1

FEBS Lett 509:161-168 (2001)

PubMed id: 11768384

The solution structure of the viral binding domain of Tva, the cellular receptor for subgroup A avian leukosis and sarcoma virus.

M.Tonelli, R.J.Peters, T.L.James, D.A.Agard.

ABSTRACT

The cellular receptor for subgroup A avian leukosis and sarcoma virus (ALSV-A) is Tva, which contains a motif related to repeats in the low density lipoprotein receptor (LDLR) ligand binding repeat (LBr) and which is necessary for viral entry. As observed with LBr repeats of LDLR, the 47 residue LBr domain of Tva (sTva47) requires calcium during oxidative folding to form the correct disulfide bonds, and calcium enhances the structure of correctly oxidized sTva47, as well as its ability to bind the viral envelope protein (Env). However, solution nuclear magnetic resonance studies indicate that, even in the presence of excess calcium, sTva47 exists in an ensemble of conformations. Nonetheless, as reported here, the structure of the predominant sTva47 solution conformer closely resembles that of other LBr repeats, with identical S-S binding topology and octahedral calcium coordination. The location of W48 and other critical residues on the surface suggests a region of the molecule necessary for Env binding and to mediate post-binding events important for ALSV-A cell entry.

Selected figure(s)

Figure 4.
Fig. 4. A: Comparison of the backbone atom coordinates of sTva47 (light blue) and LR5 (red), the fifth repeat of LDLR that was chosen as representative of the LBr domain fold (residues 24–46 of sTva47 were superimposed to residues 17–39 of LR5). B: Comparison of the calcium binding sites of sTva47 and LR5. The H-bond formed between H38 and D40 of Tva is also shown in green. The coordinates of LR5 were obtained from the PDB (1ajj). Structural comparisons were performed using the program MOLMOL [40].

Figure 5.
Fig. 5. A–C: Molecular surface of the sTva47 structure colored by electrostatic potential. In B and C, the modules are rotated vert, similar 90° around the vertical axis. This figure was prepared with the program MOLMOL [40].

The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2001, 509, 161-168) copyright 2001.

Figures were selected by an automated process.