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-Structure paper
タイトル | Interaction of decay-accelerating factor with coxsackievirus B3. |
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ジャーナル・号・ページ | J Virol, Vol. 81, Issue 23, Page 12927-12935, Year 2007 |
掲載日 | 2007年9月5日 |
著者 | Susan Hafenstein / Valorie D Bowman / Paul R Chipman / Carol M Bator Kelly / Feng Lin / M Edward Medof / Michael G Rossmann / |
PubMed 要旨 | Many entero-, parecho-, and rhinoviruses use immunoglobulin (Ig)-like receptors that bind into the viral canyon and are required to initiate viral uncoating during infection. However, some of these ...Many entero-, parecho-, and rhinoviruses use immunoglobulin (Ig)-like receptors that bind into the viral canyon and are required to initiate viral uncoating during infection. However, some of these viruses use an alternative or additional receptor that binds outside the canyon. Both the coxsackievirus-adenovirus receptor (CAR), an Ig-like molecule that binds into the viral canyon, and decay-accelerating factor (DAF) have been identified as cellular receptors for coxsackievirus B3 (CVB3). A cryoelectron microscopy reconstruction of a variant of CVB3 complexed with DAF shows full occupancy of the DAF receptor in each of 60 binding sites. The DAF molecule bridges the canyon, blocking the CAR binding site and causing the two receptors to compete with one another. The binding site of DAF on CVB3 differs from the binding site of DAF on the surface of echoviruses, suggesting independent evolutionary processes. |
リンク | J Virol / PubMed:17804498 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 14.0 - 27.0 Å |
構造データ | EMDB-1411: EMDB-1412: Interaction of decay-accelerating factor with coxsackievirus B3. |
由来 |
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キーワード | IMMUNE SYSTEM / SCR4 of DAF from 1ojv fitted into cryoEM density / Blood group antigen / Complement pathway / Glycoprotein / GPI-anchor / Immune response / Innate immunity / Lipoprotein / Membrane / Sushi / SCR1 of DAF from structure 1ojv fitted into cryoEM density / SCR2-3 of DAF fitted into cryoEM density of CVB3-RD complexed with DAF / Alternative splicing / Polymorphism |