1mr8

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{{Seed}}
 
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[[Image:1mr8.png|left|200px]]
 
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==MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN==
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The line below this paragraph, containing "STRUCTURE_1mr8", creates the "Structure Box" on the page.
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<StructureSection load='1mr8' size='340' side='right'caption='[[1mr8]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1mr8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MR8 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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{{STRUCTURE_1mr8| PDB=1mr8 | SCENE= }}
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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=1mr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mr8 OCA], [https://pdbe.org/1mr8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mr8 RCSB], [https://www.ebi.ac.uk/pdbsum/1mr8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mr8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/S10A8_HUMAN S10A8_HUMAN] S100A8 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis and adhesion. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transfering arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve proinfammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its proinflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the proinflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread.<ref>PMID:12626582</ref> <ref>PMID:15331440</ref> <ref>PMID:15598812</ref> <ref>PMID:15642721</ref> <ref>PMID:16258195</ref> <ref>PMID:19087201</ref> <ref>PMID:19122197</ref> <ref>PMID:19935772</ref> <ref>PMID:21487906</ref> <ref>PMID:22808130</ref> <ref>PMID:22363402</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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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mr/1mr8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1mr8 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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The structure of human MRP8 in the calcium-bound form was determined at 1.9 A resolution by X-ray crystallography. The structure was initially solved by MAD phasing of an ytterbium-substituted crystal and was refined against data obtained from a Ca(2+)-bound crystal. The dimeric form of MRP8 was stabilized by hydrophobic interactions between mutually wrapped helices. There were two EF-hand motifs per monomer and each EF-hand bound one Ca(2+) with a different affinity [the affinity of the C-terminal EF-hand (EF-2) for Ca(2+) was stronger than that of the N-terminal EF-hand (EF-1)]. Furthermore, replacement with Yb(3+) occurred in the C-terminal EF-hand only, suggesting a more flexible nature for EF-2 than for EF-1. This, combined with previous observations that the helix in EF-2 (helix III) undergoes a large conformational change upon calcium binding, suggests that the C-terminal EF-hand (EF-2) plays a role as a trigger for Ca(2+)-induced conformational change.
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===MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN===
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The structure of human MRP8, a member of the S100 calcium-binding protein family, by MAD phasing at 1.9 A resolution.,Ishikawa K, Nakagawa A, Tanaka I, Suzuki M, Nishihira J Acta Crystallogr D Biol Crystallogr. 2000 May;56(Pt 5):559-66. PMID:10771424<ref>PMID:10771424</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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</div>
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<div class="pdbe-citations 1mr8" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_10771424}}, adds the Publication Abstract to the page
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*[[S100 proteins 3D structures|S100 proteins 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 10771424 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10771424}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1MR8 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR8 OCA].
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==Reference==
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<ref group="xtra">PMID:10771424</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Ishikawa, K.]]
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[[Category: Large Structures]]
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[[Category: Nakagawa, A.]]
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[[Category: Ishikawa K]]
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[[Category: Nishihira, J.]]
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[[Category: Nakagawa A]]
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[[Category: Tanaka, I.]]
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[[Category: Nishihira J]]
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[[Category: Calcium-binding protein]]
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[[Category: Tanaka I]]
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[[Category: Crystal structure]]
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[[Category: Mad]]
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[[Category: Migration inhibitory factor_ related protein 8]]
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[[Category: S100 protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 11:06:58 2009''
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Current revision

MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN

PDB ID 1mr8

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