4qkw

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==Crystal structure of the zebrafish cavin4a HR1 domain==
==Crystal structure of the zebrafish cavin4a HR1 domain==
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<StructureSection load='4qkw' size='340' side='right' caption='[[4qkw]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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<StructureSection load='4qkw' size='340' side='right'caption='[[4qkw]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4qkw]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QKW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4qkw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QKW FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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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]] 1.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qkv|4qkv]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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<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=4qkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qkw OCA], [http://pdbe.org/4qkw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qkw RCSB], [http://www.ebi.ac.uk/pdbsum/4qkw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qkw ProSAT]</span></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=4qkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qkw OCA], [https://pdbe.org/4qkw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qkw RCSB], [https://www.ebi.ac.uk/pdbsum/4qkw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qkw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MURC_DANRE MURC_DANRE]] Induces rhoa activation and activates nppa transcription and myofibrillar organization through the rho/rock signaling pathway.
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[https://www.uniprot.org/uniprot/CVN4A_DANRE CVN4A_DANRE] Induces rhoa activation and activates nppa transcription and myofibrillar organization through the rho/rock signaling pathway.[UniProtKB:A2AMM0]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4qkw" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Collins, B M]]
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[[Category: Danio rerio]]
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[[Category: Kovtun, O]]
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[[Category: Large Structures]]
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[[Category: Parton, R G]]
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[[Category: Collins BM]]
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[[Category: Tillu, V]]
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[[Category: Kovtun O]]
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[[Category: Coiled-coil]]
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[[Category: Parton RG]]
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[[Category: Plasma membrane]]
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[[Category: Tillu V]]
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[[Category: Signaling protein]]
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[[Category: Signalling]]
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Current revision

Crystal structure of the zebrafish cavin4a HR1 domain

PDB ID 4qkw

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