View source for 8ybc


==Crystal structure of coiled coil domain of Golm1 (Golgi membrane protein 1)==
<StructureSection load='8ybc' size='340' side='right'caption='[[8ybc]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ybc]] 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=8YBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8YBC 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]] 2.28&#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=8ybc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ybc OCA], [https://pdbe.org/8ybc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ybc RCSB], [https://www.ebi.ac.uk/pdbsum/8ybc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ybc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GOLM1_HUMAN GOLM1_HUMAN] Unknown. Cellular response protein to viral infection.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Golgi membrane protein 1 (Golm1), a transmembrane protein with diverse subcellular localizations, has garnered significant attention in recent years due to its strong association with the development and progression of liver diseases and numerous cancers. Interestingly, although Golm1 is a membrane protein, the C-terminal of Golm1, which contains a coiled coil domain and a flexible acid region, can also be detected in the plasma of patients with various liver diseases. Notably, the coiled coil domain of serum Golm1 is postulated to play a pivotal role in physiological and pathological functions. However, little is currently known about the structure of this coiled coil domain and the full-length protein, which may limit our understanding of Golm1. Therefore, this study aims to address this gap in knowledge and reports the first crystal structure of the coiled coil domain of Golm1 at a resolution of 2.28 A. Meanwhile, we have also confirmed that the Golm1 coiled coil domain in solution can form tetramer. Our results reveal that Golm1 can form a novel tetrameric structure that differs from the previous reported dimeric structure Golm1 could assemble, which may provide novel insights into the diversity of physiological functions and pathological roles.

The first structure of human Golm1 coiled coil domain reveals an unexpected tetramer and highlights its structural diversity.,Bai W, Li B, Wu P, Li X, Huang X, Shi N, Yang C, Hu F, Xie X Int J Biol Macromol. 2024 Aug;275(Pt 1):133624. doi: , 10.1016/j.ijbiomac.2024.133624. Epub 2024 Jul 2. PMID:38964685<ref>PMID:38964685</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8ybc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bai WF]]
[[Category: Shi N]]
[[Category: Xie X]]