This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

5fmu

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

MmIFT54 CH-domain

Structural highlights

5fmu is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.593Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MIPT3_MOUSE Plays an inhibitory role on IL13 signaling by binding to IL13RA1. Involved in suppression of IL13-induced STAT6 phosphorylation, transcriptional activity and DNA-binding. Recruits TRAF3 and DISC1 to the microtubules (By similarity). Involved in epithelial morphogenesis and in the regulation of microtubule cytoskeleton organization. Is a negative regulator of microtubule stability, acting through the control of MAP4 levels (PubMed:26487268). Involved in ciliogenesis (PubMed:21945076).[UniProtKB:Q8TDR0]^[1] ^[2]

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Berbari NF, Kin NW, Sharma N, Michaud EJ, Kesterson RA, Yoder BK. Mutations in Traf3ip1 reveal defects in ciliogenesis, embryonic development, and altered cell size regulation. Dev Biol. 2011 Dec 1;360(1):66-76. doi: 10.1016/j.ydbio.2011.09.001. Epub 2011, Sep 16. PMID:21945076 doi:http://dx.doi.org/10.1016/j.ydbio.2011.09.001
↑ Bizet AA, Becker-Heck A, Ryan R, Weber K, Filhol E, Krug P, Halbritter J, Delous M, Lasbennes MC, Linghu B, Oakeley EJ, Zarhrate M, Nitschke P, Garfa-Traore M, Serluca F, Yang F, Bouwmeester T, Pinson L, Cassuto E, Dubot P, Elshakhs NA, Sahel JA, Salomon R, Drummond IA, Gubler MC, Antignac C, Chibout S, Szustakowski JD, Hildebrandt F, Lorentzen E, Sailer AW, Benmerah A, Saint-Mezard P, Saunier S. Mutations in TRAF3IP1/IFT54 reveal a new role for IFT proteins in microtubule stabilization. Nat Commun. 2015 Oct 21;6:8666. doi: 10.1038/ncomms9666. PMID:26487268 doi:http://dx.doi.org/10.1038/ncomms9666
↑ Taschner M, Weber K, Mourao A, Vetter M, Awasthi M, Stiegler M, Bhogaraju S, Lorentzen E. Intraflagellar transport proteins 172, 80, 57, 54, 38, and 20 form a stable tubulin-binding IFT-B2 complex. EMBO J. 2016 Feb 24. pii: e201593164. PMID:26912722 doi:http://dx.doi.org/10.15252/embj.201593164

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5fmu"

Categories: Large Structures | Mus musculus | Lorentzen E | Weber K

@@ Line 3: / Line 3: @@
 <StructureSection load='5fmu' size='340' side='right'caption='[[5fmu]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5fmu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FMU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FMU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5fmu]] 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=5FMU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FMU FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></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]] 1.593&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fmt|5fmt]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5fmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fmu OCA], [http://pdbe.org/5fmu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fmu RCSB], [http://www.ebi.ac.uk/pdbsum/5fmu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fmu ProSAT]</span></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=5fmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fmu OCA], [https://pdbe.org/5fmu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fmu RCSB], [https://www.ebi.ac.uk/pdbsum/5fmu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fmu ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MIPT3_MOUSE MIPT3_MOUSE]] Plays an inhibitory role on IL13 signaling by binding to IL13RA1. Involved in suppression of IL13-induced STAT6 phosphorylation, transcriptional activity and DNA-binding. Recruits TRAF3 and DISC1 to the microtubules (By similarity). Involved in epithelial morphogenesis and in the regulation of microtubule cytoskeleton organization. Is a negative regulator of microtubule stability, acting through the control of MAP4 levels (PubMed:26487268). Involved in ciliogenesis (PubMed:21945076).[UniProtKB:Q8TDR0]<ref>PMID:21945076</ref> <ref>PMID:26487268</ref>
+[https://www.uniprot.org/uniprot/MIPT3_MOUSE MIPT3_MOUSE] Plays an inhibitory role on IL13 signaling by binding to IL13RA1. Involved in suppression of IL13-induced STAT6 phosphorylation, transcriptional activity and DNA-binding. Recruits TRAF3 and DISC1 to the microtubules (By similarity). Involved in epithelial morphogenesis and in the regulation of microtubule cytoskeleton organization. Is a negative regulator of microtubule stability, acting through the control of MAP4 levels (PubMed:26487268). Involved in ciliogenesis (PubMed:21945076).[UniProtKB:Q8TDR0]<ref>PMID:21945076</ref> <ref>PMID:26487268</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 24: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Lorentzen, E]]
+[[Category: Lorentzen E]]
-[[Category: Weber, K]]
+[[Category: Weber K]]
-[[Category: Calponin homology domain]]
-[[Category: Ift]]
-[[Category: Mip-t3]]
-[[Category: Protein transport]]
-[[Category: Traf3ip1]]
-[[Category: Tubulin-binding domain]]

5fmu

From Proteopedia

Current revision

MmIFT54 CH-domain

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox