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8P2Y

Structure of human SIT1:ACE2 complex (closed PD conformation)

8P2Y の概要
エントリーDOI10.2210/pdb8p2y/pdb
EMDBエントリー17379
分子名称Processed angiotensin-converting enzyme 2, Sodium- and chloride-dependent transporter XTRP3, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
機能のキーワードcovid-19 receptor, amino acid transport, membrane protein
由来する生物種Homo sapiens (human)
詳細
タンパク質・核酸の鎖数4
化学式量合計334853.27
構造登録者
主引用文献Li, H.Z.,Pike, A.C.W.,Lotsaris, I.,Chi, G.,Hansen, J.S.,Lee, S.C.,Rodstrom, K.E.J.,Bushell, S.R.,Speedman, D.,Evans, A.,Wang, D.,He, D.,Shrestha, L.,Nasrallah, C.,Burgess-Brown, N.A.,Vandenberg, R.J.,Dafforn, T.R.,Carpenter, E.P.,Sauer, D.B.
Structure and function of the SIT1 proline transporter in complex with the COVID-19 receptor ACE2.
Nat Commun, 15:5503-5503, 2024
Cited by
PubMed Abstract: Proline is widely known as the only proteogenic amino acid with a secondary amine. In addition to its crucial role in protein structure, the secondary amino acid modulates neurotransmission and regulates the kinetics of signaling proteins. To understand the structural basis of proline import, we solved the structure of the proline transporter SIT1 in complex with the COVID-19 viral receptor ACE2 by cryo-electron microscopy. The structure of pipecolate-bound SIT1 reveals the specific sequence requirements for proline transport in the SLC6 family and how this protein excludes amino acids with extended side chains. By comparing apo and substrate-bound SIT1 states, we also identify the structural changes that link substrate release and opening of the cytoplasmic gate and provide an explanation for how a missense mutation in the transporter causes iminoglycinuria.
PubMed: 38951531
DOI: 10.1038/s41467-024-48921-x
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.46 Å)
構造検証レポート
Validation report summary of 8p2y
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-20に公開中

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