2jyo

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[[Image:2jyo.jpg|left|200px]]
 
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{{Structure
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==NMR Solution structure of Human MIP-3alpha/CCL20==
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|PDB= 2jyo |SIZE=350|CAPTION= <scene name='initialview01'>2jyo</scene>
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<StructureSection load='2jyo' size='340' side='right'caption='[[2jyo]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[2jyo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JYO FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jyo OCA], [https://pdbe.org/2jyo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jyo RCSB], [https://www.ebi.ac.uk/pdbsum/2jyo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jyo ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CCL20_HUMAN CCL20_HUMAN] Chemotactic factor that attracts lymphocytes and, slightly, neutrophils, but not monocytes. Inhibits proliferation of myeloid progenitors in colony formation assays. May be involved in formation and function of the mucosal lymphoid tissues by attracting lymphocytes and dendritic cells towards epithelial cells. C-terminal processed forms have been shown to be equally chemotactically active for leukocytes. Possesses antibacterial activity E.coli ATCC 25922 and S.aureus ATCC 29213.<ref>PMID:12149255</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jy/2jyo_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jyo ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Human macrophage inflammatory protein 3alpha (MIP-3alpha), also known as CCL20, is a 70-amino-acid chemokine which exclusively binds to chemokine receptor 6. In addition, the protein also has direct antimicrobial, antifungal, and antiviral activities. The solution structure of MIP-3alpha was solved by the use of two-dimensional homonuclear proton nuclear magnetic resonance (NMR). The structure reveals the characteristic chemokine fold, with three antiparallel beta strands followed by a C-terminal alpha helix. In contrast to the crystal structures of MIP-3alpha, the solution structure was found to be monomeric. Another difference between the NMR and crystal structures lies in the angle of the alpha helix with respect to the beta strands, which measure 69 and approximately 56.5 degrees in the two structures, respectively. NMR diffusion and pH titration studies revealed a distinct tendency for MIP-3alpha to form dimers at neutral pH and monomers at lower pH, dependent on the protonation state of His40. Molecular dynamics simulations of both the monomeric and the dimeric forms of MIP-3alpha supported the notion that the chemokine undergoes a change in helix angle upon dimerization and also highlighted the important hydrophobic and hydrogen bonding contacts made by His40 in the dimer interface. Moreover, a constrained N terminus and a smaller binding groove were observed in dimeric MIP-3alpha simulations, which could explain why monomeric MIP-3alpha may be more adept at receptor binding and activation. The solution structure of a synthetic peptide consisting of the last 20 residues of MIP-3alpha displayed a highly amphipathic alpha helix, reminiscent of various antimicrobial peptides. Antimicrobial assays with this peptide revealed strong and moderate bactericidal activities against Escherichia coli and Staphylococcus aureus, respectively. This confirms that the C-terminal alpha-helical region of MIP-3alpha plays a significant part in its broad anti-infective activity.
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'''NMR Solution structure of Human MIP-3alpha/CCL20'''
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Human macrophage inflammatory protein 3alpha: protein and peptide nuclear magnetic resonance solution structures, dimerization, dynamics, and anti-infective properties.,Chan DI, Hunter HN, Tack BF, Vogel HJ Antimicrob Agents Chemother. 2008 Mar;52(3):883-94. Epub 2007 Dec 17. PMID:18086840<ref>PMID:18086840</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==Overview==
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</div>
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Human macrophage inflammatory protein-3alpha (MIP-3alpha), also known as CCL20, is a 70 amino acid chemokine which exclusively binds to chemokine receptor 6. In addition, the protein also has direct antimicrobial, antifungal, and antiviral activities. The solution structure of MIP-3alpha was solved using two dimensional homonuclear proton NMR. The structure reveals the characteristic chemokine fold with three antiparallel beta-strands followed by a C-terminal alpha-helix. In contrast to the crystal structures of MIP-3alpha, the solution structure was found to be monomeric. Another difference between the NMR and crystal structures lies in the angle of the alpha-helix with respect to the beta-strands, measuring 69 and approximately 56.5 degrees , respectively. NMR diffusion and pH titration studies reveal a distinct tendency of MIP-3alpha to form dimers at neutral pH and monomers at lower pH, dependent on the protonation state of His 40. Molecular Dynamics simulations of both the monomeric and dimeric forms of MIP-3alpha support the notion that the chemokine undergoes a change in helix angle upon dimerization and also highlight important hydrophobic and hydrogen bonding contacts made by His 40 in the dimer interface. Moreover, a constrained N-terminus and a smaller binding groove are observed in dimeric MIP-3alpha simulations, which could explain why monomeric MIP-3alpha may be more adept at receptor binding and activation. The solution structure of a synthetic peptide consisting of the last 20 residues of MIP-3alpha displays a highly amphipathic alpha-helix, reminiscent of various antimicrobial peptides. Antimicrobial assays of this peptide reveal strong and moderate bactericidal activities against Escherichia coli and Staphylococcus aureus, respectively. This confirms that the C-terminal alpha-helical region of MIP-3alpha plays a significant part in its broad anti-infective activity.
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<div class="pdbe-citations 2jyo" style="background-color:#fffaf0;"></div>
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== References ==
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==About this Structure==
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<references/>
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2JYO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JYO OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Homo sapiens]]
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Human Macrophage Inflammatory Protein-3{alpha}: Protein and Peptide NMR Solution Structures, Dimerization, Dynamics and Anti-Infective Properties., Chan DI, Hunter HN, Tack BF, Vogel HJ, Antimicrob Agents Chemother. 2007 Dec 17;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18086840 18086840]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Chan DI]]
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[[Category: Chan, D I.]]
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[[Category: Hunter HN]]
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[[Category: Hunter, H N.]]
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[[Category: Tack BF]]
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[[Category: Tack, B F.]]
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[[Category: Vogel HJ]]
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[[Category: Vogel, H J.]]
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[[Category: alternative splicing]]
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[[Category: antibiotic]]
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[[Category: antimicrobial]]
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[[Category: chemokine]]
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[[Category: chemotaxis]]
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[[Category: cytokine]]
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[[Category: inflammatory response]]
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[[Category: polymorphism]]
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[[Category: protein]]
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[[Category: secreted]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:45:59 2008''
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Current revision

NMR Solution structure of Human MIP-3alpha/CCL20

PDB ID 2jyo

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