View source for 5yyx


==Crystal Structure of the MEK1 FHA domain==
<StructureSection load='5yyx' size='340' side='right'caption='[[5yyx]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5yyx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YYX 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]] 1.684&#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=5yyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yyx OCA], [https://pdbe.org/5yyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yyx RCSB], [https://www.ebi.ac.uk/pdbsum/5yyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yyx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MEK1_YEAST MEK1_YEAST] Probable protein kinase required for meiotic recombination.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The FHA domain-containing protein Mek1 is a meiosis-specific kinase that is involved in the regulation of interhomolog recombination in meiosis in Saccharomyces cerevisiae. The recruitment and activation of Mek1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the Mek1 FHA domain. Here, crystal structures of the Mek1 FHA domain in the apo state and in complex with the Hop1 pT318 peptide are presented, demonstrating that the hydrophobic residues Phe320 and Val321 at the pT+2 and pT+3 positions in the ligand contribute to the preferential recognition. It was further found that in Schizosaccharomyces pombe Mek1 FHA binds both pT15 in its N-terminal SQ/TQ cluster domain (SCD) and pT270 in the Hop1 SCD. The results revealed the structural basis for the preferential recognition of phosphorylated Hop1 by Mek1 in S. cerevisiae and facilitate the understanding of the interaction between the S. pombe Mek1 FHA domain and its binding targets.

Structural insights into the recognition of phosphorylated Hop1 by Mek1.,Xie C, He C, Jiang Y, Yu H, Cheng L, Nshogoza G, Ala MS, Tian C, Wu J, Shi Y, Li F Acta Crystallogr D Struct Biol. 2018 Oct 1;74(Pt 10):1027-1038. doi:, 10.1107/S2059798318011993. Epub 2018 Oct 2. PMID:30289413<ref>PMID:30289413</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5yyx" style="background-color:#fffaf0;"></div>

==See Also==
*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Jiang Y]]
[[Category: Li F]]
[[Category: Shi Y]]
[[Category: Wu J]]
[[Category: Xie C]]