5KTF
Structure of the C-terminal transmembrane domain of scavenger receptor BI (SR-BI)
Summary for 5KTF
| Entry DOI | 10.2210/pdb5ktf/pdb |
| NMR Information | BMRB: 30137 |
| Descriptor | Scavenger receptor class B member 1 (1 entity in total) |
| Functional Keywords | sr-bi, transmembrane domain, cholesterol, signaling protein |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 8185.79 |
| Authors | Chadwick, A.C.,Peterson, F.C.,Volkman, B.F.,Sahoo, D. (deposition date: 2016-07-11, release date: 2017-03-08, Last modification date: 2024-05-15) |
| Primary citation | Chadwick, A.C.,Jensen, D.R.,Hanson, P.J.,Lange, P.T.,Proudfoot, S.C.,Peterson, F.C.,Volkman, B.F.,Sahoo, D. NMR Structure of the C-Terminal Transmembrane Domain of the HDL Receptor, SR-BI, and a Functionally Relevant Leucine Zipper Motif. Structure, 25:446-457, 2017 Cited by PubMed Abstract: The interaction of high-density lipoprotein (HDL) with its receptor, scavenger receptor BI (SR-BI), is critical for lowering plasma cholesterol levels and reducing the risk for cardiovascular disease. The HDL/SR-BI complex facilitates delivery of cholesterol into cells and is likely mediated by receptor dimerization. This work describes the use of nuclear magnetic resonance (NMR) spectroscopy to generate the first high-resolution structure of the C-terminal transmembrane domain of SR-BI. This region of SR-BI harbors a leucine zipper dimerization motif, which when mutated impairs the ability of the receptor to bind HDL and mediate cholesterol delivery. These losses in function correlate with the inability of SR-BI to form dimers. We also identify juxtamembrane regions of the extracellular domain of SR-BI that may interact with the lipid surface to facilitate cholesterol transport functions of the receptor. PubMed: 28162952DOI: 10.1016/j.str.2017.01.001 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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