View source for 5xqi


==Crystal structure of full-length human Rogdi==
<StructureSection load='5xqi' size='340' side='right'caption='[[5xqi]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xqi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XQI 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]] 2.8&#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=5xqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xqi OCA], [https://pdbe.org/5xqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xqi RCSB], [https://www.ebi.ac.uk/pdbsum/5xqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xqi ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/ROGDI_HUMAN ROGDI_HUMAN] Amelo-cerebro-hypohidrotic syndrome. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/ROGDI_HUMAN ROGDI_HUMAN] May act as a positive regulator of cell proliferation.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Kohlschutter-Tonz syndrome (KTS) is a rare autosomal-recessive disorder of childhood onset characterized by global developmental delay, spasticity, epilepsy, and amelogenesis imperfecta. Rogdi, an essential protein, is highly conserved across metazoans, and mutations in Rogdi are linked to KTS. However, how certain mutations in Rogdi abolish its physiological functions and cause KTS is not known. In this study, we determined the crystal structure of human Rogdi protein at atomic resolution. Rogdi forms a novel elongated curved structure comprising the alpha domain, a leucine-zipper-like four-helix bundle, and a characteristic beta-sheet domain. Within the alpha domain, the N-terminal H1 helix (residues 19-45) pairs with the C-terminal H6 helix (residues 252-287) in an antiparallel manner, indicating that the integrity of the four-helix bundle requires both N- and C-terminal residues. The crystal structure, in conjunction with biochemical data, indicates that the alpha domain might undergo a conformational change and provide a structural platform for protein-protein interactions. Disruption of the four-helix bundle by mutation results in significant destabilization of the structure. This study provides structural insights into how certain mutations in Rogdi affect its structure and cause KTS, which has important implications for the development of pharmaceutical agents against this debilitating neurological disease.

The crystal structure of human Rogdi provides insight into the causes of Kohlschutter-Tonz Syndrome.,Lee H, Jeong H, Choe J, Jun Y, Lim C, Lee C Sci Rep. 2017 Jun 21;7(1):3972. doi: 10.1038/s41598-017-04120-x. PMID:28638151<ref>PMID:28638151</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xqi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Lee C]]
[[Category: Lee H]]