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-Structure paper
タイトル | The structure of herpesvirus fusion glycoprotein B-bilayer complex reveals the protein-membrane and lateral protein-protein interaction. |
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ジャーナル・号・ページ | Structure, Vol. 21, Issue 8, Page 1396-1405, Year 2013 |
掲載日 | 2013年8月6日 |
著者 | Ulrike E Maurer / Tzviya Zeev-Ben-Mordehai / Arun Prasad Pandurangan / Tina M Cairns / Brian P Hannah / J Charles Whitbeck / Roselyn J Eisenberg / Gary H Cohen / Maya Topf / Juha T Huiskonen / Kay Grünewald / |
PubMed 要旨 | Glycoprotein B (gB) is a key component of the complex herpesvirus fusion machinery. We studied membrane interaction of two gB ectodomain forms and present an electron cryotomography structure of the ...Glycoprotein B (gB) is a key component of the complex herpesvirus fusion machinery. We studied membrane interaction of two gB ectodomain forms and present an electron cryotomography structure of the gB-bilayer complex. The two forms differed in presence or absence of the membrane proximal region (MPR) but showed an overall similar trimeric shape. The presence of the MPR impeded interaction with liposomes. In contrast, the MPR-lacking form interacted efficiently with liposomes. Lateral interaction resulted in coat formation on the membranes. The structure revealed that interaction of gB with membranes was mediated by the fusion loops and limited to the outer membrane leaflet. The observed intrinsic propensity of gB to cluster on membranes indicates an additional role of gB in driving the fusion process forward beyond the transient fusion pore opening and subsequently leading to fusion pore expansion. |
リンク | Structure / PubMed:23850455 / PubMed Central |
手法 | EM (サブトモグラム平均) / EM (トモグラフィー) |
解像度 | 27.0 - 30.0 Å |
構造データ | EMDB-2379: |
由来 |
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キーワード | VIRAL PROTEIN / MEMBRANE PROXIMAL REGION / PROTEIN COAT / PSEUDO-ATOMIC VIRUS-HOST INTERACTION |