2xze

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[[Image:2xze.png|left|200px]]
 
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{{STRUCTURE_2xze| PDB=2xze | SCENE= }}
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==Structural basis for AMSH-ESCRT-III CHMP3 interaction==
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<StructureSection load='2xze' size='340' side='right'caption='[[2xze]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2xze]] is a 4 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=2XZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XZE 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]] 1.75&#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=2xze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xze OCA], [https://pdbe.org/2xze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xze RCSB], [https://www.ebi.ac.uk/pdbsum/2xze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xze ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/STABP_HUMAN STABP_HUMAN] Microcephaly-capillary malformation syndrome. The disease is caused by mutations affecting the gene represented in this entry.
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== Function ==
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[https://www.uniprot.org/uniprot/STABP_HUMAN STABP_HUMAN] Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains (By similarity). Plays a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF. Potentiates BMP (bone morphogenetic protein) signaling by antagonizing the inhibitory action of SMAD6 and SMAD7. Has a key role in regulation of cell surface receptor-mediated endocytosis and ubiquitin-dependent sorting of receptors to lysosomes. Endosomal localization of STAMBP is required for efficient EGFR degradation but not for its internalization (By similarity). Involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP signaling pathways.<ref>PMID:10383417</ref> <ref>PMID:11483516</ref> <ref>PMID:15314065</ref> <ref>PMID:17261583</ref> <ref>PMID:23542699</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Endosomal sorting complexes required for transport (ESCRT) recognize ubiquitinated cargo and catalyze diverse budding processes including multivesicular body biogenesis, enveloped virus egress, and cytokinesis. We present the crystal structure of an N-terminal fragment of the deubiquitinating enzyme AMSH (AMSHDeltaC) in complex with the C-terminal region of ESCRT-III CHMP3 (CHMP3DeltaN). AMSHDeltaC folds into an elongated 90 A long helical assembly that includes an unusual MIT domain. CHMP3DeltaN is unstructured in solution and helical in complex with AMSHDeltaC, revealing a novel MIT domain interacting motif (MIM) that does not overlap with the CHMP1-AMSH binding site. ITC and SPR measurements demonstrate an unusual high-affinity MIM-MIT interaction. Structural analysis suggests a regulatory role for the N-terminal helical segment of AMSHDeltaC and its destabilization leads to a loss of function during HIV-1 budding. Our results indicate a tight coupling of ESCRT-III CHMP3 and AMSH functions and provide insight into the regulation of ESCRT-III.
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===STRUCTURAL BASIS FOR AMSH-ESCRT-III CHMP3 INTERACTION===
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Structural Basis for ESCRT-III CHMP3 Recruitment of AMSH.,Solomons J, Sabin C, Poudevigne E, Usami Y, Hulsik DL, Macheboeuf P, Hartlieb B, Gottlinger H, Weissenhorn W Structure. 2011 Aug 10;19(8):1149-59. PMID:21827950<ref>PMID:21827950</ref>
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{{ABSTRACT_PUBMED_21827950}}
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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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==About this Structure==
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<div class="pdbe-citations 2xze" style="background-color:#fffaf0;"></div>
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[[2xze]] is a 4 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=2XZE OCA].
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==See Also==
==See Also==
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*[[ATPase|ATPase]]
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*[[ATPase 3D structures|ATPase 3D structures]]
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*[[Charged multivesicular body protein 3D structures|Charged multivesicular body protein 3D structures]]
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==Reference==
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== References ==
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<ref group="xtra">PMID:021827950</ref><ref group="xtra">PMID:018395747</ref><references group="xtra"/>
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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: Sabin, C.]]
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[[Category: Large Structures]]
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[[Category: Solomons, J.]]
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[[Category: Sabin C]]
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[[Category: Weissenhorn, W.]]
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[[Category: Solomons J]]
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[[Category: Hydrolase-protein transport complex]]
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[[Category: Weissenhorn W]]

Current revision

Structural basis for AMSH-ESCRT-III CHMP3 interaction

PDB ID 2xze

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