1u6d

<StructureSection load='1u6d' size='340' side='right' caption='[[1u6d]], [[Resolution|resolution]] 1.85&Aring;' scene=''>

<table><tr><td colspan='2'>[[1u6d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U6D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U6D FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Keap1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1u6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u6d OCA], [http://pdbe.org/1u6d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u6d RCSB], [http://www.ebi.ac.uk/pdbsum/1u6d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u6d ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Keap1 is a substrate adaptor protein for an ubiquitin ligase complex that targets the Nrf2 transcription factor for degradation. Keap1 binds Nrf2 through its C-terminal Kelch domain, which contains six copies of the evolutionarily conserved kelch repeat sequence motif. The structure of the Kelch domain from human Keap1 has been determined by x-ray crystallography to a resolution of 1.85 A. The Kelch domain forms a 6-bladed beta-propeller structure, with residues at the C terminus forming the first strand in the first blade. Key structural roles have been identified for the highly conserved glycine, tyrosine, and tryptophan residues that define the kelch repeat sequence motif. In addition, we show that substitution of a single amino acid located within a loop that extends out from the bottom of the beta-propeller structure abolishes binding of Nrf2. The structure of the Kelch domain of Keap1 represents a high quality model for the superfamily of eukaryotic kelch repeat proteins and provides insight into how disease-causing mutations perturb the structural integrity of the Kelch domain.

Crystal structure of the Kelch domain of human Keap1.,Li X, Zhang D, Hannink M, Beamer LJ J Biol Chem. 2004 Dec 24;279(52):54750-8. Epub 2004 Oct 8. PMID:15475350<ref>PMID:15475350</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 1u6d" style="background-color:#fffaf0;"></div>

*[[Kelch-like protein|Kelch-like protein]]

[[Category: Human]]

[[Category: Beamer, L J]]

[[Category: Hannink, M]]

[[Category: Li, X]]

[[Category: Zhang, D]]

[[Category: Protein binding]]