View source for 1uqv


==SAM domain from Ste50p==
<StructureSection load='1uqv' size='340' side='right'caption='[[1uqv]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1uqv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UQV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1uqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uqv OCA], [https://pdbe.org/1uqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uqv RCSB], [https://www.ebi.ac.uk/pdbsum/1uqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uqv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/STE50_YEAST STE50_YEAST] Involved in growth arrest during conjugation. May interact with the G protein alpha subunit.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The sterile alpha motif (SAM) is a 65-70-amino acid domain found in over 300 proteins that are involved in either signal transduction or transcriptional activation and repression. SAM domains have been shown to mediate both homodimerization and heterodimerization and in some cases oligomerization. Here, we present the solution structure of the SAM domain of the Saccharomyces cerevisiae protein, Ste50p. Ste50p functions as a modulator of the mitogen-activated protein kinase (MAPK) cascades in S. cerevisiae, which control mating, pseudohyphal growth, and osmo-tolerance. This is the first example of the structure of a SAM domain from a MAPK module protein. We have studied the associative behavior of Ste50p SAM in solution and shown that it is monomeric. We have examined the SAM domain from Ste11p, the MAPK kinase kinase that associates with Ste50p in vivo, and shown that it forms dimers with a self-association K(d) of approximately 0.5 mm. We have also analyzed the interaction of Ste50p SAM with Ste11p SAM and the effects of mutations at Val-37, Asp-38, Pro-71, Leu-73, Leu-75, and Met-99 of STE50 on the heterodimerization properties of Ste50p SAM. We have found that L73A and L75A abrogate the Ste50p interaction with Ste11p, and we compare these data with the known interaction sites defined for other SAM domain interactions.

Structure of the sterile alpha motif (SAM) domain of the Saccharomyces cerevisiae mitogen-activated protein kinase pathway-modulating protein STE50 and analysis of its interaction with the STE11 SAM.,Grimshaw SJ, Mott HR, Stott KM, Nielsen PR, Evetts KA, Hopkins LJ, Nietlispach D, Owen D J Biol Chem. 2004 Jan 16;279(3):2192-201. Epub 2003 Oct 22. PMID:14573615<ref>PMID:14573615</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1uqv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Evetts KA]]
[[Category: Grimshaw SJ]]
[[Category: Hopkins LJ]]
[[Category: Mott HR]]
[[Category: Nielsen PR]]
[[Category: Nietlispach D]]
[[Category: Owen D]]
[[Category: Stott KM]]