TY - JOUR
T1 - Conserved lipid-binding sites in membrane proteins
T2 - a focus on cytochrome c oxidase
AU - Qin, Ling
AU - Sharpe, Martyn A.
AU - Garavito, R. Michael
AU - Ferguson-Miller, Shelagh
N1 - Funding Information:
This work was supported by National Institutes of Health (NIH) Grant GM26916, Michigan State University Research Excellence Funds (REF) 03-016, and Michigan State University Foundation Strategic Partnership Grant: Quantitative Biology and Modeling Initiative (QBMI).
PY - 2007/8
Y1 - 2007/8
N2 - Specific interactions between lipids and membrane proteins have been observed in recent high-resolution crystal structures of membrane proteins. A number of cytochrome oxidase structures were analyzed, along with many amino acid sequences of membrane-spanning regions aligned according to their location in the membrane. The results reveal conservation of lipid-binding sites and of the residues that form them. These studies imply that bound lipids have important roles that are crucial to the assembly, structure, or activity of the protein. Evidence for some of these roles in subunit interactions, membrane insertion, and protein-protein complex formation is reviewed.
AB - Specific interactions between lipids and membrane proteins have been observed in recent high-resolution crystal structures of membrane proteins. A number of cytochrome oxidase structures were analyzed, along with many amino acid sequences of membrane-spanning regions aligned according to their location in the membrane. The results reveal conservation of lipid-binding sites and of the residues that form them. These studies imply that bound lipids have important roles that are crucial to the assembly, structure, or activity of the protein. Evidence for some of these roles in subunit interactions, membrane insertion, and protein-protein complex formation is reviewed.
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U2 - 10.1016/j.sbi.2007.07.001
DO - 10.1016/j.sbi.2007.07.001
M3 - Review article
C2 - 17719219
AN - SCOPUS:34548842221
SN - 0959-440X
VL - 17
SP - 444
EP - 450
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 4
ER -