PDBsum entry 4zk9

Viral protein/cytokine

PDB id: 4zk9

Contents

Protein chains

216 a.a.

61 a.a.

Ligands

NAG-NAG-BMA ×2

PDB id:

4zk9

Name:

Viral protein/cytokine

Title:

The chemokine binding protein of orf virus complexed with ccl2

Structure:

Chemokine binding protein. Chain: a. Fragment: unp residues 17-286. Engineered: yes. C-c motif chemokine 2. Chain: b. Fragment: unp residues 17-99. Synonym: hc11,monocyte chemoattractant protein 1,monocyte chemotactic and activating factor,mcaf,monocyte chemotactic protein 1,mcp-1,

Source:

Orf virus (strain nz2). Orfv. Organism_taxid: 10259. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek 293-6e. Homo sapiens. Human. Organism_taxid: 9606.

Resolution:

2.60Å R-factor: 0.241 R-free: 0.281

Authors:

K.M.Knapp,Y.Nakatani,K.L.Krause

Key ref:

R.M.Couñago et al. (2015). Structures of Orf Virus Chemokine Binding Protein in Complex with Host Chemokines Reveal Clues to Broad Binding Specificity. Structure, 23, 1199-1213. PubMed id: 26095031 DOI: 10.1016/j.str.2015.04.023

Date:

30-Apr-15 Release date: 08-Jul-15

Protein chain

Q2F862  (Q2F862_ORFN2) -  Chemokine binding protein from Orf virus (strain NZ2)

Seq: 286 a.a.

Struc: 216 a.a.

Protein chain

P13500  (CCL2_HUMAN) -  C-C motif chemokine 2 from Homo sapiens

Seq: 99 a.a.

Struc: 61 a.a.

DOI no: 10.1016/j.str.2015.04.023

Structure 23:1199-1213 (2015)

PubMed id: 26095031

Structures of Orf Virus Chemokine Binding Protein in Complex with Host Chemokines Reveal Clues to Broad Binding Specificity.

R.M.Couñago, K.M.Knapp, Y.Nakatani, S.B.Fleming, M.Corbett, L.M.Wise, A.A.Mercer, K.L.Krause.

ABSTRACT

The chemokine binding protein (CKBP) from orf virus (ORFV) binds with high affinity to chemokines from three classes, C, CC, and CXC, making it unique among poxvirus CKBPs described to date. We present its crystal structure alone and in complex with three CC chemokines, CCL2, CCL3, and CCL7. ORFV CKBP possesses a β-sandwich fold that is electrostatically and sterically complementary to its binding partners. Chemokines bind primarily through interactions involving the N-terminal loop and a hydrophobic recess on the ORFV CKBP β-sheet II surface, and largely polar interactions between the chemokine 20s loop and a negatively charged surface groove located at one end of the CKBP β-sheet II surface. ORFV CKBP interacts with leukocyte receptor and glycosaminoglycan binding sites found on the surface of bound chemokines. SEC-MALLS and chromatographic evidence is presented supporting that ORFV CKBP is a dimer in solution over a broad range of protein concentrations.