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==1.7-A resolution crystal structure of the N-terminal domain of T. brucei BILBO1==
<StructureSection load='6sjq' size='340' side='right'caption='[[6sjq]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6sjq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Trypanosoma_(trypanozoon)_brucei Trypanosoma (trypanozoon) brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SJQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SJQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mek|2mek]]</td></tr>
<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=6sjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sjq OCA], [http://pdbe.org/6sjq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sjq RCSB], [http://www.ebi.ac.uk/pdbsum/6sjq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sjq ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Trypanosoma brucei is a protist parasite causing sleeping sickness and Nagana in sub-Saharan Africa. T. brucei has a single flagellum whose base contains a bulb-like invagination of the plasma membrane called the flagellar pocket (FP). Around the neck of the FP on its cytoplasmic face is a structure called the flagellar pocket collar (FPC), which is essential for FP biogenesis. BILBO1 was the first characterized component of the FPC in trypanosomes. BILBO1's N-terminal domain (NTD) plays an essential role in T. brucei FPC biogenesis and is thus vital for the parasite's survival. Here, we report a 1.6-A resolution crystal structure of TbBILBO1-NTD, which revealed a conserved horseshoe-like hydrophobic pocket formed by an unusually long loop. Results from mutagenesis experiments suggested that another FPC protein, FPC4, interacts with TbBILBO1 by mainly contacting its three conserved aromatic residues Trp-71, Tyr-87, and Phe-89 at the center of this pocket. Our findings disclose the binding site of TbFPC4 on TbBILBO1-NTD, which may provide a basis for rational drug design targeting BILBO1 to combat T. brucei infections.

Crystal structure of the N-terminal domain of the trypanosome flagellar protein BILBO1 reveals a ubiquitin fold with a long structured loop for protein binding.,Vidilaseris K, Landrein N, Pivovarova Y, Lesigang J, Aeksiri N, Robinson DR, Bonhivers M, Dong G J Biol Chem. 2019 Dec 27. pii: RA119.010768. doi: 10.1074/jbc.RA119.010768. PMID:31882537<ref>PMID:31882537</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6sjq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Dong, G]]
[[Category: Vidilaseris, K]]
[[Category: Bilbo1]]
[[Category: Flagellar pocket collar]]
[[Category: Parasite]]
[[Category: Peptide binding protein]]
[[Category: Ubiquitin fold]]