4qkv
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4qkv]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4QKV FirstGlance]. <br> | <table><tr><td colspan='2'>[[4qkv]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4QKV 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=4qkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qkv OCA], [https://pdbe.org/4qkv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qkv RCSB], [https://www.ebi.ac.uk/pdbsum/4qkv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qkv ProSAT]</span></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]] 3Å</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=4qkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qkv OCA], [https://pdbe.org/4qkv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qkv RCSB], [https://www.ebi.ac.uk/pdbsum/4qkv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qkv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CAVN1_MOUSE CAVN1_MOUSE] Plays an important role in caveolae formation and organization. Essential for the formation of caveolae in all tissues (PubMed:18191225, PubMed:18840361, PubMed:18056712, PubMed:30188967). Core component of the CAVIN complex which is essential for recruitment of the complex to the caveolae in presence of calveolin-1 (CAV1) (PubMed:19546242). Essential for normal oligomerization of CAV1 (PubMed:23652019). Promotes ribosomal transcriptional activity in response to metabolic challenges in the adipocytes and plays an important role in the formation of the ribosomal transcriptional loop (PubMed:27528195). Dissociates transcription complexes paused by DNA-bound TTF1, thereby releasing both RNA polymerase I and pre-RNA from the template (PubMed:9582279, PubMed:11139612). The caveolae biogenesis pathway is required for the secretion of proteins such as GASK1A (PubMed:30188967).<ref>PMID:11139612</ref> <ref>PMID:18056712</ref> <ref>PMID:18191225</ref> <ref>PMID:18840361</ref> <ref>PMID:19546242</ref> <ref>PMID:23652019</ref> <ref>PMID:27528195</ref> <ref>PMID:30188967</ref> <ref>PMID:9582279</ref> | [https://www.uniprot.org/uniprot/CAVN1_MOUSE CAVN1_MOUSE] Plays an important role in caveolae formation and organization. Essential for the formation of caveolae in all tissues (PubMed:18191225, PubMed:18840361, PubMed:18056712, PubMed:30188967). Core component of the CAVIN complex which is essential for recruitment of the complex to the caveolae in presence of calveolin-1 (CAV1) (PubMed:19546242). Essential for normal oligomerization of CAV1 (PubMed:23652019). Promotes ribosomal transcriptional activity in response to metabolic challenges in the adipocytes and plays an important role in the formation of the ribosomal transcriptional loop (PubMed:27528195). Dissociates transcription complexes paused by DNA-bound TTF1, thereby releasing both RNA polymerase I and pre-RNA from the template (PubMed:9582279, PubMed:11139612). The caveolae biogenesis pathway is required for the secretion of proteins such as GASK1A (PubMed:30188967).<ref>PMID:11139612</ref> <ref>PMID:18056712</ref> <ref>PMID:18191225</ref> <ref>PMID:18840361</ref> <ref>PMID:19546242</ref> <ref>PMID:23652019</ref> <ref>PMID:27528195</ref> <ref>PMID:30188967</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. | ||
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- | 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> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 4qkv" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> |
Current revision
Crystal structure of the mouse cavin1 HR1 domain
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