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==Solution structure of SEP domain from human p47==
==Solution structure of SEP domain from human p47==
<StructureSection load='1ss6' size='340' side='right'caption='[[1ss6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='1ss6' size='340' side='right'caption='[[1ss6]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ss6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SS6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ss6]] 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=1SS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SS6 FirstGlance]. <br>
</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=1ss6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ss6 OCA], [https://pdbe.org/1ss6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ss6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ss6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ss6 ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1ss6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ss6 OCA], [https://pdbe.org/1ss6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ss6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ss6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ss6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/NSF1C_HUMAN NSF1C_HUMAN]] Reduces the ATPase activity of VCP. Necessary for the fragmentation of Golgi stacks during mitosis and for VCP-mediated reassembly of Golgi stacks after mitosis. May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER) (By similarity). Inhibits the activity of CTSL (in vitro).  
[https://www.uniprot.org/uniprot/NSF1C_HUMAN NSF1C_HUMAN] Reduces the ATPase activity of VCP. Necessary for the fragmentation of Golgi stacks during mitosis and for VCP-mediated reassembly of Golgi stacks after mitosis. May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER) (By similarity). Inhibits the activity of CTSL (in vitro).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1ss6 ConSurf].
</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=1ss6 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The solution structure of the human p47 SEP domain in a construct comprising residues G1-S2-p47(171-270) was determined by NMR spectroscopy. A structure-derived hypothesis about the domains' function was formulated and pursued in binding experiments with cysteine proteases. The SEP domain was found to be a reversible competitive inhibitor of cathepsin L with a Ki of 1.5 microM. The binding of G1-S2-p47(171-270) to cathepsin L was mapped by biochemical assays and the binding interface was investigated by NMR chemical shift perturbation experiments.
The SEP domain of p47 acts as a reversible competitive inhibitor of cathepsin L.,Soukenik M, Diehl A, Leidert M, Sievert V, Bussow K, Leitner D, Labudde D, Ball LJ, Lechner A, Nagler DK, Oschkinat H FEBS Lett. 2004 Oct 22;576(3):358-62. PMID:15498563<ref>PMID:15498563</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ss6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ball, L J]]
[[Category: Ball LJ]]
[[Category: Buessow, K]]
[[Category: Buessow K]]
[[Category: Labudde, D]]
[[Category: Labudde D]]
[[Category: Leidert, M]]
[[Category: Leidert M]]
[[Category: Leitner, D]]
[[Category: Leitner D]]
[[Category: Oschkinat, H]]
[[Category: Oschkinat H]]
[[Category: Sievert, V]]
[[Category: Sievert V]]
[[Category: Soukenik, M]]
[[Category: Soukenik M]]
[[Category: Nmr]]
[[Category: P47]]
[[Category: Sep]]
[[Category: Signaling protein]]

Revision as of 08:34, 1 May 2024

Solution structure of SEP domain from human p47

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