3kbl

<table><tr><td colspan='2'>[[3kbl]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KBL FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3k6t|3k6t]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gld-1, T23G11.3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</td></tr>

[[https://www.uniprot.org/uniprot/GLD1_CAEEL GLD1_CAEEL]] Germ line-specific tumor suppressor essential for oogenesis. Controls the spatial pattern of translation of multiple oogenesis specific mRNAs (e.g. yolk receptor rme-2) by repression of translation during early meiotic prophase (leptotene to pachytene) and then derepression of translation during diplotene/ diakinesis, following its degradation. Also functions to promote the male sexual fate in the hermaphrodite germline but not the male germline. Functions redundantly with gld-2 to promote the initiation of meiotic development and/or inhibit stem cell proliferation.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Posttranscriptional regulation of gene expression is an important mechanism for modulating protein levels in eukaryotes, especially in developmental pathways. The highly conserved homodimeric STAR/GSG proteins play a key role in regulating translation by binding bipartite consensus sequences in the untranslated regions of target mRNAs, but the exact mechanism remains unknown. Structures of STAR protein RNA binding subdomains have been determined, but structural information is lacking for the homodimerization subdomain. Here, we present the structure of the C. elegans GLD-1 homodimerization domain dimer, determined by a combination of X-ray crystallography and NMR spectroscopy, revealing a helix-turn-helix monomeric fold with the two protomers stacked perpendicularly. Structure-based mutagenesis demonstrates that the dimer interface is not easily disrupted, but the structural integrity of the monomer is crucial for GLD-1 dimerization. Finally, an improved model for STAR-mediated translational regulation of mRNA, based on the GLD-1 homodimerization domain structure, is presented.

Structure of the GLD-1 homodimerization domain: insights into STAR protein-mediated translational regulation.,Beuck C, Szymczyna BR, Kerkow DE, Carmel AB, Columbus L, Stanfield RL, Williamson JR Structure. 2010 Mar 10;18(3):377-89. PMID:20223220<ref>PMID:20223220</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 3kbl" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Caeel]]

[[Category: Beuck, C]]

[[Category: Carmel, A B]]

[[Category: Columbus, L]]

[[Category: Kerkow, D E]]

[[Category: Stanfield, R L]]

[[Category: Szymczyna, B R]]

[[Category: Williamson, J R]]

[[Category: Translation regulation]]