4Y5D
CRYSTAL STRUCTURE OF ALiS2-STREPTAVIDIN COMPLEX
Summary for 4Y5D
Entry DOI | 10.2210/pdb4y5d/pdb |
Related | 4Y59 |
Descriptor | Streptavidin, methyl 3-(4-oxo-4,5-dihydrofuro[3,2-c]pyridin-2-yl)benzoate, 3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL, ... (6 entities in total) |
Functional Keywords | biotin-binding protein, inhibitor |
Biological source | Streptomyces avidinii |
Total number of polymer chains | 4 |
Total formula weight | 53492.95 |
Authors | Sugiyama, S.,Terai, T.,Kohno, M.,Ishida, H.,Nagano, T. (deposition date: 2015-02-11, release date: 2015-09-23, Last modification date: 2024-03-20) |
Primary citation | Terai, T.,Kohno, M.,Boncompain, G.,Sugiyama, S.,Saito, N.,Fujikake, R.,Ueno, T.,Komatsu, T.,Hanaoka, K.,Okabe, T.,Urano, Y.,Perez, F.,Nagano, T. Artificial Ligands of Streptavidin (ALiS): Discovery, Characterization, and Application for Reversible Control of Intracellular Protein Transport J.Am.Chem.Soc., 137:10464-10467, 2015 Cited by PubMed Abstract: Artificial ligands of streptavidin (ALiS) with association constants of ∼10(6) M(-1) were discovered by high-throughput screening of our chemical library, and their binding characteristics, including X-ray crystal structure of the streptavidin complex, were determined. Unlike biotin and its derivatives, ALiS exhibits fast dissociation kinetics and excellent cell permeability. The streptavidin-ALiS system provides a novel, practical compound-dependent methodology for repeated reversible cycling of protein localization between intracellular organella. PubMed: 26261872DOI: 10.1021/jacs.5b05672 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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