5TCX
Crystal structure of human tetraspanin CD81
5TCX の概要
| エントリーDOI | 10.2210/pdb5tcx/pdb |
| 分子名称 | CD81 antigen, CHOLESTEROL (3 entities in total) |
| 機能のキーワード | tetraspanin, transmembrane, cholesterol, cell invasion |
| 由来する生物種 | Homo sapiens (Human) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 27590.24 |
| 構造登録者 | Zimmerman, B.,McMillan, B.J.,Seegar, T.C.M.,Kruse, A.C.,Blacklow, S.C. (登録日: 2016-09-16, 公開日: 2016-11-09, 最終更新日: 2023-10-04) |
| 主引用文献 | Zimmerman, B.,Kelly, B.,McMillan, B.J.,Seegar, T.C.,Dror, R.O.,Kruse, A.C.,Blacklow, S.C. Crystal Structure of a Full-Length Human Tetraspanin Reveals a Cholesterol-Binding Pocket. Cell, 167:1041-1051.e11, 2016 Cited by PubMed Abstract: Tetraspanins comprise a diverse family of four-pass transmembrane proteins that play critical roles in the immune, reproductive, genitourinary, and auditory systems. Despite their pervasive roles in human physiology, little is known about the structure of tetraspanins or the molecular mechanisms underlying their various functions. Here, we report the crystal structure of human CD81, a full-length tetraspanin. The transmembrane segments of CD81 pack as two largely separated pairs of helices, capped by the large extracellular loop (EC2) at the outer membrane leaflet. The two pairs of helices converge at the inner leaflet to create an intramembrane pocket with additional electron density corresponding to a bound cholesterol molecule within the cavity. Molecular dynamics simulations identify an additional conformation in which EC2 separates substantially from the transmembrane domain. Cholesterol binding appears to modulate CD81 activity in cells, suggesting a potential mechanism for regulation of tetraspanin function. PubMed: 27881302DOI: 10.1016/j.cell.2016.09.056 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.955 Å) |
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