View source for 7yfv


==Structure of Rpgrip1l CC1==
<StructureSection load='7yfv' size='340' side='right'caption='[[7yfv]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7yfv]] is a 4 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=7YFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YFV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=7yfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yfv OCA], [https://pdbe.org/7yfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yfv RCSB], [https://www.ebi.ac.uk/pdbsum/7yfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yfv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FTM_MOUSE FTM_MOUSE] Negatively regulates signaling through the G-protein coupled thromboxane A2 receptor (TBXA2R) (By similarity). May be involved in mechanisms like programmed cell death, craniofacial development, patterning of the limbs, and formation of the left-right axis. Involved in the organization of apical junctions; the function is proposed to implicate a NPHP1-4-8 module. Does not seem to be strictly required for ciliogenesis (By similarity). Involved in establishment of planar cell polarity such as in cochlear sensory epithelium and is proposed to implicate stabilization of disheveled proteins (PubMed:22927466). Involved in regulation of proteasomal activity at the primary cilium probably implicating association with PSDM2 (PubMed:26150391).[UniProtKB:Q68CZ1]<ref>PMID:10501967</ref> <ref>PMID:11956760</ref> <ref>PMID:21565611</ref> <ref>PMID:22927466</ref> <ref>PMID:26150391</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Rpgrip1l is one of the key ciliary proteins located at the transition zone of the primary cilium, an important organelle for cells to sense the outer environment. Mutations in the RPGRIP1L gene are associated with various ciliopathies. Here, we focused on the N-terminal coiled-coil of Rpgrip1l. By comprehensive biochemical and structural characterizations, we demonstrated that the two predicted coiled-coil regions (CC12) located at Rpgrip1l N-terminus each can form a stable parallel dimer. We further showed that overexpression of Rpgrip1l CC12 in NIH/3T3 cells significantly shortened the length of primary cilia, and this effect depended on the dimer formation. In addition, we found that CC12 of the homolog protein Rpgrip1 in mouse and human were significantly different from Rpgrip1l. Finally, we confirmed that some disease-related mutations can alter the dimeric states of CC12 of Rpgrip1l or Rpgrip1, which might explain the pathogenic mechanisms.

Structure of the N-terminal coiled-coil domains of the ciliary protein Rpgrip1l.,He R, Chen G, Li Z, Li J iScience. 2023 Feb 21;26(3):106249. doi: 10.1016/j.isci.2023.106249. eCollection , 2023 Mar 17. PMID:36915689<ref>PMID:36915689</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7yfv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Chen G]]
[[Category: He R]]
[[Category: Li J]]
[[Category: Li Z]]