1apl

<table><tr><td colspan='2'>[[1apl]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1APL FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MAT ALPHA2 RES. 128-210 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1apl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apl OCA], [http://pdbe.org/1apl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1apl RCSB], [http://www.ebi.ac.uk/pdbsum/1apl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1apl ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/MTAL2_YEAST MTAL2_YEAST]] Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Transcriptional corepressor that binds cooperatively with MCM1 to a 31-basepair DNA sequence termed the a-specific gene (asg) operator, to repress the transcription of a-cell-specific genes. Additionally, in a/alpha diploid cells, binds cooperatively with the A1 protein to a 21-basepair DNA sequence termed the haploid-specific gene (hsg) operator, to repress transcription of haploid-specific genes and of MATALPHA1.<ref>PMID:8664541</ref>

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== Publication Abstract from PubMed ==

The MAT alpha 2 homeodomain regulates the expression of cell type-specific genes in yeast. We have determined the 2.7 A resolution crystal structure of the alpha 2 homeodomain bound to a biologically relevant DNA sequence. The DNA in this complex is contacted primarily by the third of three alpha-helices, with additional contacts coming from an N-terminal arm. Comparison of the yeast alpha 2 and the Drosophila engrailed homeodomain-DNA complexes shows that the protein fold is highly conserved, despite a 3-residue insertion in alpha 2 and only 27% sequence identity between the two homeodomains. Moreover, the orientation of the recognition helix on the DNA is also conserved. This docking arrangement is maintained by side chain contacts with the DNA--primarily the sugar-phosphate backbone--that are identical in alpha 2 and engrailed. Since these residues are conserved among all homeodomains, we propose that the contacts with the DNA are also conserved and suggest a general model for homeodomain-DNA interactions.

Crystal structure of a MAT alpha 2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions.,Wolberger C, Vershon AK, Liu B, Johnson AD, Pabo CO Cell. 1991 Nov 1;67(3):517-28. PMID:1682054<ref>PMID:1682054</ref>

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

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<div class="pdbe-citations 1apl" style="background-color:#fffaf0;"></div>

[[Category: Atcc 18824]]

[[Category: Johnson, A D]]

[[Category: Liu, B]]

[[Category: Pabo, C O]]

[[Category: Vershon, A K]]

[[Category: Wolberger, C]]

[[Category: Protein-dna complex]]