|
|
| Line 1: |
Line 1: |
| | | | |
| | ==The chemokine binding protein of orf virus complexed with CCL3== | | ==The chemokine binding protein of orf virus complexed with CCL3== |
| - | <StructureSection load='4zkb' size='340' side='right' caption='[[4zkb]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='4zkb' size='340' side='right'caption='[[4zkb]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4zkb]] 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=4ZKB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZKB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zkb]] 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=4ZKB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZKB 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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zk9|4zk9]], [[4zkc|4zkc]]</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=4zkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zkb OCA], [https://pdbe.org/4zkb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zkb RCSB], [https://www.ebi.ac.uk/pdbsum/4zkb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zkb ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CCL3, G0S19-1, MIP1A, SCYA3 ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4zkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zkb OCA], [http://pdbe.org/4zkb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zkb RCSB], [http://www.ebi.ac.uk/pdbsum/4zkb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zkb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CCL3_HUMAN CCL3_HUMAN]] Monokine with inflammatory and chemokinetic properties. Binds to CCR1, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant MIP-1-alpha induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV).<ref>PMID:8525373</ref> | + | [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 == |
| Line 24: |
Line 22: |
| | __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: Ccl3]]
| + | |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Orf 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.
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
|
