3eab: Difference between revisions

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 ==Crystal structure of Spastin MIT in complex with ESCRT III==
-<StructureSection load='3eab' size='340' side='right' caption='[[3eab]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<StructureSection load='3eab' size='340' side='right'caption='[[3eab]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3eab]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EAB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3eab]] is a 12 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=3EAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EAB FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPAST, KIAA1083, SPG4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 2.5&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3eab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eab OCA], [http://pdbe.org/3eab PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3eab RCSB], [http://www.ebi.ac.uk/pdbsum/3eab PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3eab 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=3eab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eab OCA], [https://pdbe.org/3eab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eab RCSB], [https://www.ebi.ac.uk/pdbsum/3eab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eab ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/SPAST_HUMAN SPAST_HUMAN]] Defects in SPAST are the cause of spastic paraplegia autosomal dominant type 4 (SPG4) [MIM:[http://omim.org/entry/182601 182601]]. Spastic paraplegia is a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG4 is the most common form of autosomal dominant spastic paraplegias.<ref>PMID:11809724</ref> <ref>PMID:15716377</ref> <ref>PMID:17389232</ref> <ref>PMID:19000169</ref> <ref>PMID:16339213</ref> <ref>PMID:15891913</ref> <ref>PMID:10610178</ref> <ref>PMID:11039577</ref> <ref>PMID:10699187</ref> <ref>PMID:11015453</ref> <ref>PMID:11087788</ref> <ref>PMID:11309678</ref> <ref>PMID:12460147</ref> <ref>PMID:11843700</ref> <ref>PMID:12124993</ref> <ref>PMID:12161613</ref> <ref>PMID:11985387</ref> <ref>PMID:12163196</ref> <ref>PMID:12202986</ref> <ref>PMID:12552568</ref> <ref>PMID:12939659</ref> <ref>PMID:14732620</ref> <ref>PMID:15210521</ref> <ref>PMID:15248095</ref> <ref>PMID:15482961</ref> <ref>PMID:15159500</ref> <ref>PMID:15326248</ref> <ref>PMID:16682546</ref> <ref>PMID:16684598</ref> <ref>PMID:17594340</ref> <ref>PMID:20214791</ref> <ref>PMID:20932283</ref> <ref>PMID:20562464</ref> <ref>PMID:20718791</ref> <ref>PMID:20550563</ref>
+[https://www.uniprot.org/uniprot/SPAST_HUMAN SPAST_HUMAN] Defects in SPAST are the cause of spastic paraplegia autosomal dominant type 4 (SPG4) [MIM:[https://omim.org/entry/182601 182601]. Spastic paraplegia is a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG4 is the most common form of autosomal dominant spastic paraplegias.<ref>PMID:11809724</ref> <ref>PMID:15716377</ref> <ref>PMID:17389232</ref> <ref>PMID:19000169</ref> <ref>PMID:16339213</ref> <ref>PMID:15891913</ref> <ref>PMID:10610178</ref> <ref>PMID:11039577</ref> <ref>PMID:10699187</ref> <ref>PMID:11015453</ref> <ref>PMID:11087788</ref> <ref>PMID:11309678</ref> <ref>PMID:12460147</ref> <ref>PMID:11843700</ref> <ref>PMID:12124993</ref> <ref>PMID:12161613</ref> <ref>PMID:11985387</ref> <ref>PMID:12163196</ref> <ref>PMID:12202986</ref> <ref>PMID:12552568</ref> <ref>PMID:12939659</ref> <ref>PMID:14732620</ref> <ref>PMID:15210521</ref> <ref>PMID:15248095</ref> <ref>PMID:15482961</ref> <ref>PMID:15159500</ref> <ref>PMID:15326248</ref> <ref>PMID:16682546</ref> <ref>PMID:16684598</ref> <ref>PMID:17594340</ref> <ref>PMID:20214791</ref> <ref>PMID:20932283</ref> <ref>PMID:20562464</ref> <ref>PMID:20718791</ref> <ref>PMID:20550563</ref>
 == Function ==
-[[http://www.uniprot.org/uniprot/SPAST_HUMAN SPAST_HUMAN]] ATP-dependent microtubule severing protein. Microtubule severing may promote reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and for completion of the abscission stage of cytokinesis. May also play a role in axon growth and the formation of axonal branches.<ref>PMID:11809724</ref> <ref>PMID:12676568</ref> <ref>PMID:15716377</ref> <ref>PMID:16219033</ref> <ref>PMID:17389232</ref> <ref>PMID:19000169</ref>
+[https://www.uniprot.org/uniprot/SPAST_HUMAN SPAST_HUMAN] ATP-dependent microtubule severing protein. Microtubule severing may promote reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and for completion of the abscission stage of cytokinesis. May also play a role in axon growth and the formation of axonal branches.<ref>PMID:11809724</ref> <ref>PMID:12676568</ref> <ref>PMID:15716377</ref> <ref>PMID:16219033</ref> <ref>PMID:17389232</ref> <ref>PMID:19000169</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 21: / Line 21: @@
 </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=3eab ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The endosomal sorting complex required for transport (ESCRT) machinery, including ESCRT-III, localizes to the midbody and participates in the membrane-abscission step of cytokinesis. The ESCRT-III protein charged multivesicular body protein 1B (CHMP1B) is required for recruitment of the MIT domain-containing protein spastin, a microtubule-severing enzyme, to the midbody. The 2.5-A structure of the C-terminal tail of CHMP1B with the MIT domain of spastin reveals a specific, high-affinity complex involving a noncanonical binding site between the first and third helices of the MIT domain. The structural interface is twice as large as that of the MIT domain of the VPS4-CHMP complex, consistent with the high affinity of the interaction. A series of unique hydrogen-bonding interactions and close packing of small side chains discriminate against the other ten human ESCRT-III subunits. Point mutants in the CHMP1B binding site of spastin block recruitment of spastin to the midbody and impair cytokinesis.
-Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B.,Yang D, Rismanchi N, Renvoise B, Lippincott-Schwartz J, Blackstone C, Hurley JH Nat Struct Mol Biol. 2008 Dec;15(12):1278-86. Epub 2008 Nov 9. PMID:18997780<ref>PMID:18997780</ref>
+==See Also==
+*[[Charged multivesicular body protein 3D structures|Charged multivesicular body protein 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3eab" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Blackstone, C]]
+[[Category: Large Structures]]
-[[Category: Hurley, J H]]
+[[Category: Blackstone C]]
-[[Category: Lippincott-Schwartz, J]]
+[[Category: Hurley JH]]
-[[Category: Renvoise, B]]
+[[Category: Lippincott-Schwartz J]]
-[[Category: Rimanchi, N]]
+[[Category: Renvoise B]]
-[[Category: Yang, D]]
+[[Category: Rimanchi N]]
-[[Category: Alternative splicing]]
+[[Category: Yang D]]
-[[Category: Atp-binding]]
-[[Category: Cell cycle]]
-[[Category: Chmp]]
-[[Category: Cytoplasm]]
-[[Category: Disease mutation]]
-[[Category: Escrt]]
-[[Category: Hereditary spastic paraplegia]]
-[[Category: Mit]]
-[[Category: Nucleotide-binding]]
-[[Category: Nucleus]]
-[[Category: Polymorphism]]
-[[Category: Spastin]]