4gqb

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[[Image:4gqb.png|left|200px]]
 
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{{STRUCTURE_4gqb| PDB=4gqb | SCENE= }}
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==Crystal Structure of the human PRMT5:MEP50 Complex==
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<StructureSection load='4gqb' size='340' side='right'caption='[[4gqb]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4gqb]] is a 3 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=4GQB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GQB 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]] 2.06&#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=0XU:(2S,5S,6E)-2,5-DIAMINO-6-[(3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3,4-DIHYDROXYDIHYDROFURAN-2(3H)-YLIDENE]HEXANOIC+ACID'>0XU</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
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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=4gqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gqb OCA], [https://pdbe.org/4gqb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gqb RCSB], [https://www.ebi.ac.uk/pdbsum/4gqb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gqb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ANM5_HUMAN ANM5_HUMAN] Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. Plays a role in the assembly of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. May regulate the SUPT5H transcriptional elongation properties. May be part of a pathway that is connected to a chloride current, possibly through cytoskeletal rearrangement. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage. Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation. Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9. Methylates and regulates SRGAP2 which is involved in cell migration and differentiation. Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter.<ref>PMID:10531356</ref> <ref>PMID:11152681</ref> <ref>PMID:11747828</ref> <ref>PMID:12411503</ref> <ref>PMID:15737618</ref> <ref>PMID:17709427</ref> <ref>PMID:20159986</ref> <ref>PMID:20810653</ref> <ref>PMID:21258366</ref> <ref>PMID:21917714</ref> <ref>PMID:22269951</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Protein arginine methyltransferases (PRMTs) play important roles in several cellular processes, including signaling, gene regulation, and transport of proteins and nucleic acids, to impact growth, differentiation, proliferation, and development. PRMT5 symmetrically di-methylates the two-terminal omega-guanidino nitrogens of arginine residues on substrate proteins. PRMT5 acts as part of a multimeric complex in concert with a variety of partner proteins that regulate its function and specificity. A core component of these complexes is the WD40 protein MEP50/WDR77/p44, which mediates interactions with binding partners and substrates. We have determined the crystal structure of human PRMT5 in complex with MEP50 (methylosome protein 50), bound to an S-adenosylmethionine analog and a peptide substrate derived from histone H4. The structure of the surprising hetero-octameric complex reveals the close interaction between the seven-bladed beta-propeller MEP50 and the N-terminal domain of PRMT5, and delineates the structural elements of substrate recognition.
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===Crystal Structure of the human PRMT5:MEP50 Complex===
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Crystal structure of the human PRMT5:MEP50 complex.,Antonysamy S, Bonday Z, Campbell RM, Doyle B, Druzina Z, Gheyi T, Han B, Jungheim LN, Qian Y, Rauch C, Russell M, Sauder JM, Wasserman SR, Weichert K, Willard FS, Zhang A, Emtage S Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17960-5. doi:, 10.1073/pnas.1209814109. Epub 2012 Oct 15. PMID:23071334<ref>PMID:23071334</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 4gqb" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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[[4gqb]] is a 3 chain structure with sequence 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=4GQB OCA].
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*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Antonysamy, S.]]
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[[Category: Large Structures]]
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[[Category: Bonday, Z.]]
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[[Category: Antonysamy S]]
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[[Category: Campbell, R.]]
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[[Category: Bonday Z]]
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[[Category: Doyle, B.]]
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[[Category: Campbell R]]
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[[Category: Druzina, Z.]]
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[[Category: Doyle B]]
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[[Category: Emtage, S.]]
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[[Category: Druzina Z]]
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[[Category: Gheyi, T.]]
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[[Category: Emtage S]]
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[[Category: Han, B.]]
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[[Category: Gheyi T]]
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[[Category: Jungheim, L N.]]
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[[Category: Han B]]
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[[Category: Qian, Y.]]
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[[Category: Jungheim LN]]
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[[Category: Rauch, C.]]
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[[Category: Qian Y]]
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[[Category: Russell, M.]]
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[[Category: Rauch C]]
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[[Category: Sauder, J M.]]
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[[Category: Russell M]]
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[[Category: Wasserman, S R.]]
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[[Category: Sauder JM]]
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[[Category: Weichert, K.]]
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[[Category: Wasserman SR]]
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[[Category: Willard, F S.]]
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[[Category: Weichert K]]
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[[Category: Zhang, A.]]
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[[Category: Willard FS]]
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[[Category: Beta-propeller]]
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[[Category: Zhang A]]
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[[Category: Methylation]]
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[[Category: Methyltransferase]]
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[[Category: Tim barrel]]
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[[Category: Transferase-protein binding complex]]
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Current revision

Crystal Structure of the human PRMT5:MEP50 Complex

PDB ID 4gqb

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