7T2Q

PEGylated Calmodulin-1 (K148U)

Summary for 7T2Q

• Entry DOI: 10.2210/pdb7t2q/pdb
• Descriptor: Calmodulin-1, CALCIUM ION, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: calmodulin-1, metal binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 17073.59

Authors

Mackay, J.P.,Payne, R.J.,Patel, K.,Dowman, L.J. (deposition date: 2021-12-06, release date: 2022-10-26, Last modification date: 2023-10-25)

Primary citation

Dowman, L.J.,Kulkarni, S.S.,Alegre-Requena, J.V.,Giltrap, A.M.,Norman, A.R.,Sharma, A.,Gallegos, L.C.,Mackay, A.S.,Welegedara, A.P.,Watson, E.E.,van Raad, D.,Niederacher, G.,Huhmann, S.,Proschogo, N.,Patel, K.,Larance, M.,Becker, C.F.W.,Mackay, J.P.,Lakhwani, G.,Huber, T.,Paton, R.S.,Payne, R.J.
Site-selective photocatalytic functionalization of peptides and proteins at selenocysteine.
Nat Commun, 13:6885-6885, 2022

PubMed Abstract: The importance of modified peptides and proteins for applications in drug discovery, and for illuminating biological processes at the molecular level, is fueling a demand for efficient methods that facilitate the precise modification of these biomolecules. Herein, we describe the development of a photocatalytic method for the rapid and efficient dimerization and site-specific functionalization of peptide and protein diselenides. This methodology, dubbed the photocatalytic diselenide contraction, involves irradiation at 450 nm in the presence of an iridium photocatalyst and a phosphine and results in rapid and clean conversion of diselenides to reductively stable selenoethers. A mechanism for this photocatalytic transformation is proposed, which is supported by photoluminescence spectroscopy and density functional theory calculations. The utility of the photocatalytic diselenide contraction transformation is highlighted through the dimerization of selenopeptides, and by the generation of two families of protein conjugates via the site-selective modification of calmodulin containing the 21 amino acid selenocysteine, and the C-terminal modification of a ubiquitin diselenide.

PubMed: 36371402
DOI: 10.1038/s41467-022-34530-z

Experimental method

X-RAY DIFFRACTION (1.95 Å)