1z1v: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1z1v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z1V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z1V FirstGlance]. <br> | <table><tr><td colspan='2'>[[1z1v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z1V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z1V FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1uqv|1uqv]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1uqv|1uqv]]</td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STE50 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STE50 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z1v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1z1v RCSB], [http://www.ebi.ac.uk/pdbsum/1z1v PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z1v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1z1v RCSB], [http://www.ebi.ac.uk/pdbsum/1z1v PDBsum]</span></td></tr> | ||
<table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 18824]] | [[Category: Atcc 18824]] | ||
[[Category: Donaldson, L W | [[Category: Donaldson, L W]] | ||
[[Category: Kwan, J J | [[Category: Kwan, J J]] | ||
[[Category: Maini, J | [[Category: Maini, J]] | ||
[[Category: Pawson, T | [[Category: Pawson, T]] | ||
[[Category: Warner, N | [[Category: Warner, N]] | ||
[[Category: All helix protein]] | [[Category: All helix protein]] | ||
[[Category: Cell cycle]] | [[Category: Cell cycle]] | ||
[[Category: Sam domain]] | [[Category: Sam domain]] | ||
Revision as of 01:42, 4 January 2015
NMR structure of the Saccharomyces cerevisiae Ste50 SAM domainNMR structure of the Saccharomyces cerevisiae Ste50 SAM domain
Structural highlights
Publication Abstract from PubMedIn Saccharomyces cerevisiae, signal transduction through pathways governing mating, osmoregulation, and nitrogen starvation depends upon a direct interaction between the sterile alpha motif (SAM) domains of the Ste11 mitogen-activated protein kinase kinase kinase (MAPKKK) and its regulator Ste50. Previously, we solved the NMR structure of the SAM domain from Ste11 and identified two mutants that diminished binding to the Ste50 SAM domain. Building upon the Ste11 study, we present the NMR structure of the monomeric Ste50 SAM domain and a series of mutants bearing substitutions at surface-exposed hydrophobic amino acid residues. The mid-loop (ML) region of Ste11-SAM, defined by helices H3 and H4 and the end-helix (EH) region of Ste50-SAM, defined by helix H5, were sensitive to substitution, indicating that these two surfaces contribute to the high-affinity interaction. The combination of two mutants, Ste11-SAM-L72R and Ste50-SAM-L69R, formed a high-affinity heterodimer unencumbered by competing homotypic interactions that had prevented earlier NMR studies of the wild-type complex. Yeast bearing mutations that prevented the heterotypic Ste11-Ste50 association in vitro presented signaling defects in the mating and high-osmolarity growth pathways. Saccharomyces cerevisiae Ste50 binds the MAPKKK Ste11 through a head-to-tail SAM domain interaction.,Kwan JJ, Warner N, Maini J, Chan Tung KW, Zakaria H, Pawson T, Donaldson LW J Mol Biol. 2006 Feb 10;356(1):142-54. Epub 2005 Nov 28. PMID:16337230[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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