PDBsum entry 4zkb

Viral protein/cytokine

PDB id: 4zkb

Contents

Protein chains

218 a.a.

49 a.a.

Ligands

NAG-NAG

NAG-NAG-BMA

PDB id:

4zkb

Name:

Viral protein/cytokine

Title:

The chemokine binding protein of orf virus complexed with ccl3

Structure:

Chemokine binding protein. Chain: a. Fragment: unp residues 17-286. Engineered: yes. C-c motif chemokine 3. Chain: b. Fragment: unp residues 24-92. Synonym: g0/g1 switch regulatory protein 19-1,macrophage inflammatory protein 1-alpha,mip-1-alpha,pat 464.1,sis-beta,small-inducible

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:

2.90Å R-factor: 0.270 R-free: 0.323

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: 218 a.a.

Protein chain

P10147  (CCL3_HUMAN) -  C-C motif chemokine 3 from Homo sapiens

Seq: 92 a.a.

Struc: 49 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.