5b4n
From Proteopedia
Structure analysis of function associated loop mutant of substrate recognition domain of Fbs1 ubiquitin ligase
Structural highlights
FunctionFBX44_HUMAN Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.FBX2_MOUSE Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Involved in the endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins by recognizing and binding sugar chains on unfolded glycoproteins that are retrotranslocated into the cytosol and promoting their ubiquitination and subsequent degradation. Prevents formation of cytosolic aggregates of unfolded glycoproteins that have been retrotranslocated into the cytosol. Able to recognize and bind denatured glycoproteins, preferentially those of the high-mannose type.[1] [2] [3] [4] [5] Publication Abstract from PubMedThe SCF ubiquitin ligase comprises four components: Skp1, Cul1, Rbx1 and a variable-subunit F-box protein. The F-box protein Fbs1, which recognizes the N-linked glycoproteins, is involved in the endoplasmic reticulum-associated degradation pathway. Although FBG3, another F-box protein, shares 51% sequence identity with Fbs1, FBG3 does not bind glycoproteins. To investigate the sequence-structure relationship of the substrate-binding pocket, the crystal structure of a mutant substrate-binding domain of Fbs1 in which the six nonconserved regions (beta1, beta2-beta3, beta3-beta4, beta5-beta6, beta7-beta8 and beta9-beta10) of Fbs1 were substituted with those of FBG3 was determined. The substrate-binding pocket of this model exhibits structural features that differ from those of Fsb1. Structural analysis of a function-associated loop mutant of the substrate-recognition domain of Fbs1 ubiquitin ligase.,Nishio K, Yoshida Y, Tanaka K, Mizushima T Acta Crystallogr F Struct Biol Commun. 2016 Aug;72(Pt 8):619-26. doi:, 10.1107/S2053230X16011018. Epub 2016 Jul 27. PMID:27487926[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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