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| | ==The chemokine binding protein of orf virus complexed with CCL2== | | ==The chemokine binding protein of orf virus complexed with CCL2== |
| - | <StructureSection load='4zk9' size='340' side='right' caption='[[4zk9]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='4zk9' size='340' side='right'caption='[[4zk9]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4zk9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Orfn2 Orfn2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZK9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZK9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zk9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Orf_virus_(strain_NZ2) Orf virus (strain NZ2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZK9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZK9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zkb|4zkb]], [[4zkc|4zkc]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CCL2, MCP1, SCYA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4zk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zk9 OCA], [https://pdbe.org/4zk9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zk9 RCSB], [https://www.ebi.ac.uk/pdbsum/4zk9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zk9 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4zk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zk9 OCA], [http://pdbe.org/4zk9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zk9 RCSB], [http://www.ebi.ac.uk/pdbsum/4zk9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zk9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CCL2_HUMAN CCL2_HUMAN]] Chemotactic factor that attracts monocytes and basophils but not neutrophils or eosinophils. Augments monocyte anti-tumor activity. Has been implicated in the pathogenesis of diseases characterized by monocytic infiltrates, like psoriasis, rheumatoid arthritis or atherosclerosis. May be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis. | + | [https://www.uniprot.org/uniprot/Q2F862_ORFV Q2F862_ORFV] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| | *[[Monocyte chemoattractant protein|Monocyte chemoattractant protein]] | | *[[Monocyte chemoattractant protein|Monocyte chemoattractant protein]] |
| - | *[[User:Coline Perrin/CCL2|User:Coline Perrin/CCL2]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Orfn2]] | + | [[Category: Large Structures]] |
| - | [[Category: Knapp, K M]] | + | [[Category: Knapp KM]] |
| - | [[Category: Krause, K L]] | + | [[Category: Krause KL]] |
| - | [[Category: Nakatani, Y]] | + | [[Category: Nakatani Y]] |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Human c-c motif chemokine 2]]
| + | |
| - | [[Category: Orf virus chemokine binding protein]]
| + | |
| - | [[Category: Viral protein-cytokine complex]]
| + | |
| Structural highlights
Function
Q2F862_ORFV
Publication Abstract from PubMed
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 beta-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 beta-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 beta-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.
Structures of Orf Virus Chemokine Binding Protein in Complex with Host Chemokines Reveal Clues to Broad Binding Specificity.,Counago RM, Knapp KM, Nakatani Y, Fleming SB, Corbett M, Wise LM, Mercer AA, Krause KL Structure. 2015 Jun 10. pii: S0969-2126(15)00192-6. doi:, 10.1016/j.str.2015.04.023. PMID:26095031[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Counago RM, Knapp KM, Nakatani Y, Fleming SB, Corbett M, Wise LM, Mercer AA, Krause KL. Structures of Orf Virus Chemokine Binding Protein in Complex with Host Chemokines Reveal Clues to Broad Binding Specificity. Structure. 2015 Jun 10. pii: S0969-2126(15)00192-6. doi:, 10.1016/j.str.2015.04.023. PMID:26095031 doi:http://dx.doi.org/10.1016/j.str.2015.04.023
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