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-Structure paper
タイトル | Structure of the human Meckel-Gruber protein Meckelin. |
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ジャーナル・号・ページ | Sci Adv, Vol. 7, Issue 45, Page eabj9748, Year 2021 |
掲載日 | 2021年11月5日 |
著者 | Dongliang Liu / Dandan Qian / Huaizong Shen / Deshun Gong / |
PubMed 要旨 | Mutations in the gene account for most cases of the Meckel-Gruber syndrome, the most severe ciliopathy with a 100% mortality rate. Here, we report a 3.3-Å cryo–electron microscopy structure of ...Mutations in the gene account for most cases of the Meckel-Gruber syndrome, the most severe ciliopathy with a 100% mortality rate. Here, we report a 3.3-Å cryo–electron microscopy structure of human Meckelin (also known as TMEM67 and MKS3). The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain. Meckelin forms a stable homodimer with an extensive dimer interface. Our structure establishes a framework for dissecting the function and disease mechanisms of Meckelin. |
リンク | Sci Adv / PubMed:34731008 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.34 Å |
構造データ | EMDB-31584, PDB-7fh1: |
由来 |
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キーワード | MEMBRANE PROTEIN / Cryo-EM |