4qkv
From Proteopedia
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| - | ''' | + | ==Crystal structure of the mouse cavin1 HR1 domain== |
| + | <StructureSection load='4qkv' size='340' side='right' caption='[[4qkv]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4qkv]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QKV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QKV FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qkw|4qkw]]</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=4qkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qkv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qkv RCSB], [http://www.ebi.ac.uk/pdbsum/4qkv PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PTRF_MOUSE PTRF_MOUSE]] Plays an important role in caveolae formation and organization. Required for the sequestration of mobile caveolin into immobile caveolae. Termination of transcription by RNA polymerase I involves pausing of transcription by TTF1, and the dissociation of the transcription complex, releasing pre-rRNA and RNA polymerase I from the template. PTRF is required for dissociation of the ternary transcription complex.<ref>PMID:11139612</ref> <ref>PMID:18056712</ref> <ref>PMID:18191225</ref> <ref>PMID:18840361</ref> <ref>PMID:9582279</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Caveolae are cell-surface membrane invaginations that play critical roles in cellular processes including signaling and membrane homeostasis. The cavin proteins, in cooperation with caveolins, are essential for caveola formation. Here we show that a minimal N-terminal domain of the cavins, termed HR1, is required and sufficient for their homo- and hetero-oligomerization. Crystal structures of the mouse cavin1 and zebrafish cavin4a HR1 domains reveal highly conserved trimeric coiled-coil architectures, with intersubunit interactions that determine the specificity of cavin-cavin interactions. The HR1 domain contains a basic surface patch that interacts with polyphosphoinositides and coordinates with additional membrane-binding sites within the cavin C terminus to facilitate membrane association and remodeling. Electron microscopy of purified cavins reveals the existence of large assemblies, composed of a repeating rod-like structural element, and we propose that these structures polymerize through membrane-coupled interactions to form the unique striations observed on the surface of caveolae in vivo. | ||
| - | + | Structural insights into the organization of the cavin membrane coat complex.,Kovtun O, Tillu VA, Jung W, Leneva N, Ariotti N, Chaudhary N, Mandyam RA, Ferguson C, Morgan GP, Johnston WA, Harrop SJ, Alexandrov K, Parton RG, Collins BM Dev Cell. 2014 Nov 24;31(4):405-19. doi: 10.1016/j.devcel.2014.10.002. Epub 2014 , Nov 13. PMID:25453557<ref>PMID:25453557</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Collins, B M]] | ||
| + | [[Category: Kovtun, O]] | ||
| + | [[Category: Parton, R G]] | ||
[[Category: Tillu, V]] | [[Category: Tillu, V]] | ||
| - | [[Category: | + | [[Category: Coiled-coil]] |
| - | [[Category: | + | [[Category: Plasma membrane]] |
| - | [[Category: | + | [[Category: Signalling]] |
| + | [[Category: Transcription]] | ||
Revision as of 12:02, 18 March 2015
Crystal structure of the mouse cavin1 HR1 domain
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