PDBsum entry 1v9u

Virus/receptor

PDB id: 1v9u

Contents

Protein chains

269 a.a. *

250 a.a. *

237 a.a. *

25 a.a. *

39 a.a. *

Ligands

DAO

Metals

_CA

* Residue conservation analysis

References listed in PDB file

Key reference

Title

X-Ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein.

Authors

N.Verdaguer, I.Fita, M.Reithmayer, R.Moser, D.Blaas.

Ref.

Nat Struct Mol Biol, 2004, 11, 429-434. [DOI no: 10.1038/nsmb753]

PubMed id

15064754

Abstract

Although many viral receptors have been identified, the ways in which they interact with their cognate viruses are not understood at the molecular level. We have determined the X-ray structure of a complex between calcium-containing modules of the very low-density lipoprotein receptor and the minor group human rhinovirus HRV2. The receptor binds close to the icosahedral five-fold vertex, with only one module per virus protomer. The binding face of this module is defined by acidic calcium-chelating residues and, in particular, by an exposed tryptophan that is highly conserved. The attachment site on the virus involves only residues from VP1, particularly a lysine strictly conserved in all minor group HRVs. The disposition of the attached ligand-binding repeats around the five-fold axis, together with the proximity of the N- and C-terminal ends of adjacent modules, suggests that more than one repeat in a single receptor molecule might attach simultaneously.

Figure 1.
Figure 1. Scheme of the modular organization of members of the LDLR family. LDLR and VLDLR have seven and eight N-terminal ligand binding repeats, L1 -L7 and V1 -V8, respectively. Three epidermal growth factor precursor-like regions (A -C) flank a six-bladed -propeller ( ) with YWTD motifs. The adjacent domain (GLYCO) carries O-linked oligosaccharides. The receptors are anchored in the membrane via a single transmembrane domain (TM). The intracellular C termini carry NPXY clathrin-localization signals.

Figure 2.
Figure 2. Three-dimensional structure of the V23 -HRV2 complex. (a) Stereo view of the 3.5 Å -averaged electron density of V3 bound to HRV2. The region corresponds to residues from His13 to Glu36 of the V3 receptor. The V3 model is also shown in ball-and-stick representation. The Ca^2+ ion in the center of the acidic cluster is green. Residues involved directly in interactions with HRV2 are labeled. (b) Orthogonal views of an HRV2-V3 pentamer subunit. HRV2 proteins are shown as space-filling model colored in the standard viral protein color code (VP1, blue, VP2, green and VP3, red) in the reference protomer and light blue in the others. The five V3 receptors are shown as worms in yellow.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Mol Biol (2004, 11, 429-434) copyright 2004.