3v32: Difference between revisions

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<StructureSection load='3v32' size='340' side='right'caption='[[3v32]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3v32' size='340' side='right'caption='[[3v32]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3v32]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V32 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3v32]] 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=3V32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V32 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3v33|3v33]], [[3v34|3v34]]</div></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&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MCPIP1 ([https://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=3v32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v32 OCA], [https://pdbe.org/3v32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v32 RCSB], [https://www.ebi.ac.uk/pdbsum/3v32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v32 ProSAT]</span></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=3v32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v32 OCA], [https://pdbe.org/3v32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v32 RCSB], [https://www.ebi.ac.uk/pdbsum/3v32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v32 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ZC12A_HUMAN ZC12A_HUMAN]] Has RNase activity and selectively degrades specific target mRNA species. Modulates the immune response and inflammation by regulating the decay of specific mRNA molecules. Recognizes the 3'-untranslated region (UTR) of the mRNA for IL6, CALCR and IL12B. Required for normal decay of IL6 mRNA (By similarity). Triggers apoptosis and promotes angiogenesis in response to the binding of CCL2 to CCR2. Regulates expression of CDH12 and CHD19.<ref>PMID:16574901</ref> <ref>PMID:18364357</ref> <ref>PMID:22561375</ref> 
[https://www.uniprot.org/uniprot/ZC12A_HUMAN ZC12A_HUMAN] Has RNase activity and selectively degrades specific target mRNA species. Modulates the immune response and inflammation by regulating the decay of specific mRNA molecules. Recognizes the 3'-untranslated region (UTR) of the mRNA for IL6, CALCR and IL12B. Required for normal decay of IL6 mRNA (By similarity). Triggers apoptosis and promotes angiogenesis in response to the binding of CCL2 to CCR2. Regulates expression of CDH12 and CHD19.<ref>PMID:16574901</ref> <ref>PMID:18364357</ref> <ref>PMID:22561375</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
MCP-1-induced protein 1 (MCPIP1) plays an important role in the downregulation of the LPS-induced immune response by acting as an RNase targeting IL-6 and IL-12b mRNAs. A conserved domain located in the N-terminal part of MCPIP1 is thought to be responsible for its RNase activity, but its catalytic mechanism is not well understood due to the lack of an atomic resolution structure. We determined the 3D crystal structure of this MCPIP1 N-terminal conserved RNase domain at a resolution of 2.0 A. The overall structure of MCPIP1 N-terminal conserved domain shares high structural homology with PilT N-terminal domain. We show that the RNase catalytic center is composed of several acidic residues, verifying their importance by site-specific mutagenesis. A positively charged arm close to the catalytic center may act as an RNA substrate-binding site, since exchange of critical positively charged residues on this arm with alanine partially abolish the RNase activity of MCPIP1 in vivo. Our structure of the MCPIP1 N-terminal conserved domain reveals the details of the catalytic center and provides a greater understanding of the RNA degradation mechanism.
 
Structural study of MCPIP1 N-terminal conserved domain reveals a PIN-like RNase.,Xu J, Peng W, Sun Y, Wang X, Xu Y, Li X, Gao G, Rao Z Nucleic Acids Res. 2012 May 4. PMID:22561375<ref>PMID:22561375</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3v32" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Gao, G]]
[[Category: Gao G]]
[[Category: Li, X]]
[[Category: Li X]]
[[Category: Peng, W]]
[[Category: Peng W]]
[[Category: Rao, Z]]
[[Category: Rao Z]]
[[Category: Sun, Y]]
[[Category: Sun Y]]
[[Category: Wang, X]]
[[Category: Wang X]]
[[Category: Xu, J]]
[[Category: Xu J]]
[[Category: Xu, Y]]
[[Category: Xu Y]]
[[Category: Cytoplastic]]
[[Category: Hydrolase]]
[[Category: Rnase]]
[[Category: Rossmann-like sandwich fold]]

Latest revision as of 11:39, 20 March 2024

Crystal structure of MCPIP1 N-terminal conserved domainCrystal structure of MCPIP1 N-terminal conserved domain

Structural highlights

3v32 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ZC12A_HUMAN Has RNase activity and selectively degrades specific target mRNA species. Modulates the immune response and inflammation by regulating the decay of specific mRNA molecules. Recognizes the 3'-untranslated region (UTR) of the mRNA for IL6, CALCR and IL12B. Required for normal decay of IL6 mRNA (By similarity). Triggers apoptosis and promotes angiogenesis in response to the binding of CCL2 to CCR2. Regulates expression of CDH12 and CHD19.[1] [2] [3]

See Also

References

  1. ↑ Zhou L, Azfer A, Niu J, Graham S, Choudhury M, Adamski FM, Younce C, Binkley PF, Kolattukudy PE. Monocyte chemoattractant protein-1 induces a novel transcription factor that causes cardiac myocyte apoptosis and ventricular dysfunction. Circ Res. 2006 May 12;98(9):1177-85. Epub 2006 Mar 30. PMID:16574901 doi:http://dx.doi.org/10.1161/01.RES.0000220106.64661.71
  2. ↑ Niu J, Azfer A, Zhelyabovska O, Fatma S, Kolattukudy PE. Monocyte chemotactic protein (MCP)-1 promotes angiogenesis via a novel transcription factor, MCP-1-induced protein (MCPIP). J Biol Chem. 2008 May 23;283(21):14542-51. doi: 10.1074/jbc.M802139200. Epub 2008, Mar 24. PMID:18364357 doi:http://dx.doi.org/10.1074/jbc.M802139200
  3. ↑ Xu J, Peng W, Sun Y, Wang X, Xu Y, Li X, Gao G, Rao Z. Structural study of MCPIP1 N-terminal conserved domain reveals a PIN-like RNase. Nucleic Acids Res. 2012 May 4. PMID:22561375 doi:10.1093/nar/gks359

3v32, resolution 2.00Å

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