9fmn

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m (Protected "9fmn" [edit=sysop:move=sysop])
Current revision (04:05, 5 October 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9fmn is ON HOLD
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==Structure of Human PADI6==
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<StructureSection load='9fmn' size='340' side='right'caption='[[9fmn]], [[Resolution|resolution]] 2.44&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9fmn]] 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=9FMN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FMN 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]] 2.44&#8491;</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=9fmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9fmn OCA], [https://pdbe.org/9fmn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9fmn RCSB], [https://www.ebi.ac.uk/pdbsum/9fmn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9fmn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PADI6_HUMAN PADI6_HUMAN] Catalyzes the deimination of arginine residues of proteins. May be involved in cytoskeletal reorganization in the egg and early embryo (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Peptidyl arginine deiminase 6 (PADI6 or PAD6) is vital for early embryonic development in mice and humans, yet its function remains elusive. PADI6 is less conserved than other PADIs and it is currently unknown whether it has a catalytic function. Here we show that human PADI6 dimerises like hPADIs 2-4, however, does not bind Ca(2+) and is inactive in in vitro assays against standard PADI substrates. By determining the crystal structure of hPADI6, we show that hPADI6 is structured in the absence of Ca(2+) where hPADI2 and hPADI4 are not, and the Ca-binding sites are not conserved. Moreover, we show that whilst the key catalytic aspartic acid and histidine residues are structurally conserved, the cysteine is displaced far from the active site centre and the hPADI6 active site pocket appears closed through a unique evolved mechanism in hPADI6, not present in the other PADIs. Taken together, these findings provide insight into how the function of hPADI6 may differ from the other PADIs based on its structure and provides a resource for characterising the damaging effect of clinically significant PADI6 variants.
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Authors: Mouilleron, S., Walport, L., Williams, J., Marsh, A.J., Hernandez Trapero, R.
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Structural insight into the function of human peptidyl arginine deiminase 6.,Williams JPC, Mouilleron S, Trapero RH, Bertran MT, Marsh JA, Walport LJ Comput Struct Biotechnol J. 2024 Aug 16;23:3258-3269. doi: , 10.1016/j.csbj.2024.08.019. eCollection 2024 Dec. PMID:39286527<ref>PMID:39286527</ref>
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Description: Structure of Human PADI6
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Marsh, A.J]]
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<div class="pdbe-citations 9fmn" style="background-color:#fffaf0;"></div>
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[[Category: Hernandez Trapero, R]]
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== References ==
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[[Category: Mouilleron, S]]
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<references/>
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[[Category: Williams, J]]
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__TOC__
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[[Category: Walport, L]]
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Hernandez Trapero R]]
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[[Category: Marsh AJ]]
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[[Category: Mouilleron S]]
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[[Category: Walport L]]
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[[Category: Williams J]]

Current revision

Structure of Human PADI6

PDB ID 9fmn

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