Structural Characterization of the Intra- and Inter-Repeat Copper Binding Modes within the N-Terminal Region of “Prion Related Protein” (PrP-rel-2) of Zebrafish

2008 ◽  
Vol 112 (47) ◽  
pp. 15140-15150 ◽  
Author(s):  
Elena Gaggelli ◽  
Elzbieta Jankowska ◽  
Henryk Kozlowski ◽  
Alina Marcinkowska ◽  
Caterina Migliorini ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Terminal Region ◽  
Copper Binding ◽  
Binding Modes ◽  
Related Protein

scholarly journals KCTD proteins as Cullin3 E3 Ligase adapters

2014 ◽  
Vol 70 (a1) ◽  
pp. C305-C305
Author(s):  
Alan Ji ◽  
Gilbert Privé
Keyword(s):  
Crystal Structure ◽  
Structural Characterization ◽  
Dissociation Constants ◽  
E3 Ligase ◽  
Terminal Region ◽  
Btb Domain ◽  
Substrate Protein ◽  
Ubiquitin E3 Ligase ◽  
Ubiquitin Moiety

Cullin3 (Cul3) is an ubiquitin E3 ligase responsible for catalyzing the transfer of an ubiquitin moiety from an E2 enzyme to a target substrate protein. The C-terminal region of Cul3 binds RBX1/E2-ubiquitin, while, the N-terminal region interacts with various BTB domain proteins which serve as substrate adaptors. Previously, our group determined the crystal structures of the homodimeric BTB proteins SPOP and KLHL3 in complex with the N-terminal domain of Cul3, revealing the determinants responsible for the BTB/Cul3 interaction [1, 2]. A second class of BTB-domain containing proteins, the KCTD proteins, are also Cul3 substrate adaptors but these do not share many of the previously determined features for Cul3 binding. Furthermore, KCTD proteins form homotetramers and homopentamers via BTB oligomerization rather than the previously described homodimers. Despite these differences, many KCTD proteins interact with Cul3 with dissociation constants of approximately 50 nM. While the target substrates for many of the KCTD/Cul3 E3 ligase complexes are unknown, recent studies have implicated the GABAβ2 receptor as an interactor of KCTD 8, 12, 12b and 16. Here, we report the pentameric crystal structure of the KCTD9 BTB domain and our progress on the structural characterization of Cul3/KCTD/substrate complexes.

Cloning and characterization of a fourth human lysyl oxidase isoenzyme

2001 ◽  
Vol 355 (2) ◽  
pp. 381-387 ◽  
Author(s):  
Joni M. MÄKI ◽  
Kari I. KIVIRIKKO
Keyword(s):  
Nuclear Localization Signal ◽  
Culture Medium ◽  
Lysyl Oxidase ◽  
Scavenger Receptor ◽  
Terminal Region ◽  
Copper Binding ◽  
Tyrosine Residues ◽  
Localization Signal ◽  
Binding Sequence

We report here the complete cDNA sequence and exon-intron organization of the human lysyl oxidase-like (LOXL)3 gene, a new member of the lysyl oxidase (LO) gene family. The predicted polypeptide is 753 amino acids in length, including a signal peptide of 25 residues. The C-terminal region, residues 529-729, contains a LO domain similar to those in the LOX (the first characterized LO isoenzyme), LOXL and LOXL2 polypeptides. It possesses the putative copper binding sequence, and the lysine and tyrosine residues that form the lysyltyrosyl quinone cofactor. The N-terminal region, which is similar to that in LOXL2 but not those in LOX and LOXL, contains four subregions similar to scavenger receptor cysteine-rich domains and a putative nuclear localization signal. Recombinant LOXL3, expressed in HT-1080 cells, was secreted into the culture medium but was not detected by immunofluorescence staining in nuclei. The LOXL3 mRNA is 3.1kb in size and is expressed in many tissues, the highest levels among the tissues studied being seen in the placenta, heart, ovary, testis, small intestine and spleen.

scholarly journals Structural Characterization of Natural Nickel and Copper Binding Ligands along the US GEOTRACES Eastern Pacific Zonal Transect

2016 ◽  
Vol 3 ◽  
Author(s):  
Rene M. Boiteau ◽  
Claire P. Till ◽  
Angel Ruacho ◽  
Randelle M. Bundy ◽  
Nicholas J. Hawco ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Eastern Pacific ◽  
Copper Binding ◽  
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