Phospholipid-induced structural changes to an erythroid [beta] spectrin ankyrin-dependent lipid-binding site Export

@article{citeulike:3177376, abstract = {The region of [beta]-spectrin that is responsible for interactions with ankyrin was shown to comprise an ankyrin-sensitive lipid-binding site. Structural studies indicate that it exhibits a mixed 310/[alpha] helical conformation and is highly amphipathic. These features together with the distinctively conserved sequence of the lipid-binding site motivated us to explore the mechanism of its interactions with biological membranes. A series of singly and doubly spin-labeled erythroid [beta]-spectrin-derived peptides was constructed, and the spin-label mobility and spin-spin distances were analyzed via electron paramagnetic resonance spectroscopy and two different calculation methods. The results indicate that in [beta]-spectrin, the lipid-binding domain, which is part of the 14th segment, has the topology of typical triple-helical spectrin repeat. However, it undergoes significant changes when interacting with phospholipids or detergents. A mechanism for these interactions is proposed in this paper.}, author = {Czogalla, Aleksander and Grzymajlo, Krzysztof and Jezierski, Adam and Sikorski, Aleksander F.}, citeulike-article-id = {3177376}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.bbamem.2008.07.020}, citeulike-linkout-1 = {http://www.sciencedirect.com/science/article/B6T1T-4T4Y5XY-1/2/571f42630883cb1d052ca006c93451ca}, doi = {10.1016/j.bbamem.2008.07.020}, journal = {Biochimica et Biophysica Acta (BBA) - Biomembranes}, keywords = {interaction, lipids, membrane, phospholipids, protein}, posted-at = {2008-09-01 04:42:26}, priority = {2}, title = {Phospholipid-induced structural changes to an erythroid [beta] spectrin ankyrin-dependent lipid-binding site}, url = {http://dx.doi.org/10.1016/j.bbamem.2008.07.020}, volume = {In Press, Uncorrected Proof} }

TY - JOUR ID - citeulike:3177376 L3 - citeulike-article-id:3177376 N2 - The region of [beta]-spectrin that is responsible for interactions with ankyrin was shown to comprise an ankyrin-sensitive lipid-binding site. Structural studies indicate that it exhibits a mixed 310/[alpha] helical conformation and is highly amphipathic. These features together with the distinctively conserved sequence of the lipid-binding site motivated us to explore the mechanism of its interactions with biological membranes. A series of singly and doubly spin-labeled erythroid [beta]-spectrin-derived peptides was constructed, and the spin-label mobility and spin-spin distances were analyzed via electron paramagnetic resonance spectroscopy and two different calculation methods. The results indicate that in [beta]-spectrin, the lipid-binding domain, which is part of the 14th segment, has the topology of typical triple-helical spectrin repeat. However, it undergoes significant changes when interacting with phospholipids or detergents. A mechanism for these interactions is proposed in this paper. JF - Biochimica et Biophysica Acta (BBA) - Biomembranes TI - Phospholipid-induced structural changes to an erythroid [beta] spectrin ankyrin-dependent lipid-binding site VL - In Press, Uncorrected Proof KW - interaction KW - lipids KW - membrane KW - phospholipids KW - protein AU - Czogalla, Aleksander AU - Grzymajlo, Krzysztof AU - Jezierski, Adam AU - Sikorski, Aleksander UR - http://dx.doi.org/10.1016/j.bbamem.2008.07.020 ER -