View source for 5fms


==mmIFT52 N-terminal domain==
<StructureSection load='5fms' size='340' side='right'caption='[[5fms]], [[Resolution|resolution]] 3.49&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5fms]] 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=5FMS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FMS 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]] 3.488&#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=5fms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fms OCA], [https://pdbe.org/5fms PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fms RCSB], [https://www.ebi.ac.uk/pdbsum/5fms PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fms ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IFT52_MOUSE IFT52_MOUSE] Forms part of a complex involved in intraflagellar transport (IFT), the bi-directional movement of particles required for the assembly, maintenance and functioning of primary cilia.<ref>PMID:19253336</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Intraflagellar transport (IFT) relies on the IFT complex and is required for ciliogenesis. The IFT-B complex consists of 9-10 stably associated core subunits and six "peripheral" subunits that were shown to dissociate from the core structure at moderate salt concentration. We purified the six "peripheral" IFT-B subunits of Chlamydomonas reinhardtii as recombinant proteins and show that they form a stable complex independently of the IFT-B core. We suggest a nomenclature of IFT-B1 (core) and IFT-B2 (peripheral) for the two IFT-B subcomplexes. We demonstrate that IFT88, together with the N-terminal domain of IFT52, is necessary to bridge the interaction between IFT-B1 and B2. The crystal structure of IFT52N reveals highly conserved residues critical for IFT-B1/IFT-B2 complex formation. Furthermore, we show that of the three IFT-B2 subunits containing a calponin homology (CH) domain (IFT38, 54, and 57), only IFT54 binds alphabeta-tubulin as a potential IFT cargo, whereas the CH domains of IFT38 and IFT57 mediate the interaction with IFT80 and IFT172, respectively. Crystal structures of IFT54 CH domains reveal that tubulin binding is mediated by basic surface-exposed residues.

Intraflagellar transport proteins 172, 80, 57, 54, 38, and 20 form a stable tubulin-binding IFT-B2 complex.,Taschner M, Weber K, Mourao A, Vetter M, Awasthi M, Stiegler M, Bhogaraju S, Lorentzen E EMBO J. 2016 Feb 24. pii: e201593164. PMID:26912722<ref>PMID:26912722</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5fms" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Lorentzen E]]
[[Category: Mourao A]]