Kelch-like protein
From Proteopedia
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<StructureSection load='4ifl' size='340' side='right' caption='Human Kelch-like protein19 (Keap1) Kelch domain (dark green) complex with NRF2 Neh2 peptide (light green) (PDB code [[4ifl]])' scene=''> | <StructureSection load='4ifl' size='340' side='right' caption='Human Kelch-like protein19 (Keap1) Kelch domain (dark green) complex with NRF2 Neh2 peptide (light green) (PDB code [[4ifl]])' scene=''> | ||
== Function == | == Function == | ||
| - | '''Kelch-like proteins''' (KLHL) contain multiple Kelch motifs. This motif is about 50 residues long and forms a four-stranded β-sheet blade. Six to | + | '''Kelch-like proteins''' (KLHL) contain multiple Kelch motifs. This motif is about 50 residues long and forms a four-stranded β-sheet blade. Six to eight such blades form a circular β-propeller domain. β-propellers are involved in protein-protein interactions. The N-terminal of KLHL contains other protein domains like BTB (Broad-Tramtrack-Bric-a-brac) which is also involved in protein-protein interactions<ref>PMID:23676014</ref>. |
== Disease == | == Disease == | ||
| + | Somatic mutations in Keap1 were found in lung cancer patients. | ||
== Relevance == | == Relevance == | ||
| - | |||
'''KLHL19 (Keap1)''' interacts with the Neh2 peptide of NRF2. NRF2 is a regulator of antioxidant response, hence Keap1 is investigated as a drug target. | '''KLHL19 (Keap1)''' interacts with the Neh2 peptide of NRF2. NRF2 is a regulator of antioxidant response, hence Keap1 is investigated as a drug target. | ||
== Structural highlights == | == Structural highlights == | ||
| + | The interaction of Keap1 with Neh2 is through the first Glu in the latter's ETGE motif<ref>PMID:16507366</ref>. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:24, 5 April 2016
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3D Structures of Kelch-like protein
Updated on 05-April-2016
References
- ↑ Dhanoa BS, Cogliati T, Satish AG, Bruford EA, Friedman JS. Update on the Kelch-like (KLHL) gene family. Hum Genomics. 2013 May 15;7:13. doi: 10.1186/1479-7364-7-13. PMID:23676014 doi:http://dx.doi.org/10.1186/1479-7364-7-13
- ↑ Padmanabhan B, Tong KI, Ohta T, Nakamura Y, Scharlock M, Ohtsuji M, Kang MI, Kobayashi A, Yokoyama S, Yamamoto M. Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer. Mol Cell. 2006 Mar 3;21(5):689-700. PMID:16507366 doi:10.1016/j.molcel.2006.01.013
