Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4ZKB

The chemokine binding protein of orf virus complexed with CCL3

Summary for 4ZKB
Entry DOI10.2210/pdb4zkb/pdb
Related4ZK9 4ZKC
DescriptorChemokine binding protein, C-C motif chemokine 3, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordscomplex, orf chemokine binding protein, ccl3, viral protein-cytokine complex, viral protein/cytokine
Biological sourceOrf virus (strain NZ2) (ORFV)
More
Total number of polymer chains2
Total formula weight39937.02
Authors
Knapp, K.M.,Nakatani, Y.,Krause, K.L. (deposition date: 2015-04-30, release date: 2015-07-08, Last modification date: 2023-09-27)
Primary citationCounago, R.M.,Knapp, K.M.,Nakatani, Y.,Fleming, S.B.,Corbett, M.,Wise, L.M.,Mercer, A.A.,Krause, K.L.
Structures of Orf Virus Chemokine Binding Protein in Complex with Host Chemokines Reveal Clues to Broad Binding Specificity.
Structure, 23:1199-1213, 2015
Cited by
PubMed 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.
PubMed: 26095031
DOI: 10.1016/j.str.2015.04.023
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9 Å)
Structure validation

226707

건을2024-10-30부터공개중

PDB statisticsPDBj update infoContact PDBjnumon