Cargando…
Identification of allosteric disulfides from labile bonds in X-ray structures
Protein disulfide bonds link pairs of cysteine sulfur atoms and are either structural or functional motifs. The allosteric disulfides control the function of the protein in which they reside when cleaved or formed. Here, we identify potential allosteric disulfides in all Protein Data Bank X-ray stru...
Autores principales: | Pijning, Aster E., Chiu, Joyce, Yeo, Reichelle X., Wong, Jason W. H., Hogg, Philip J. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society Publishing
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5830721/ https://www.ncbi.nlm.nih.gov/pubmed/29515832 http://dx.doi.org/10.1098/rsos.171058 |
Ejemplares similares
-
Search for allosteric disulfide bonds in NMR structures
por: Schmidt, Bryan, et al.
Publicado: (2007) -
One-Way Allosteric Communication between the Two Disulfide Bonds in Tissue Factor
por: Zhou, Beifei, et al.
Publicado: (2017) -
The role of the disulfide bond in the interaction of islet amyloid polypeptide with membranes
por: Khemtémourian, Lucie, et al.
Publicado: (2010) -
Labile disulfide bonds are common at the leucocyte cell surface
por: Metcalfe, Clive, et al.
Publicado: (2011) -
Mechano-redox control of integrin de-adhesion
por: Passam, Freda, et al.
Publicado: (2018)