TY - JOUR
T1 - Structure of the uncleaved ectodomain of the paramyxovirus (hPIV3) fusion protein
AU - Yin, Hsien Sheng
AU - Paterson, Reay G.
AU - Wen, Xiaolin
AU - Lamb, Robert A.
AU - Jardetzky, Theodore S.
N1 - Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2005/6/28
Y1 - 2005/6/28
N2 - Class I viral fusion proteins share common mechanistic and structural features but little sequence similarity. Structural insights into the protein conformational changes associated with membrane fusion are based largely on studies of the influenza virus hemagglutinin in pre- and postfusion conformations. Here, we present the crystal structure of the secreted, uncleaved ectodomain of the paramyxovirus, human parainfluenza virus 3 fusion (F) protein, a member of the class I viral fusion protein group. The secreted human parainfluenza virus 3 F forms a trimer with distinct head, neck, and stalk regions. Unexpectedly, the structure reveals a six-helix bundle associated with the postfusion form of F, suggesting that the anchor-minus ectodomain adopts a conformation largely similar to the postfusion state. The transmembrane anchor domains of F may therefore profoundly influence the folding energetics that establish and maintain a metastable, prefusion state.
AB - Class I viral fusion proteins share common mechanistic and structural features but little sequence similarity. Structural insights into the protein conformational changes associated with membrane fusion are based largely on studies of the influenza virus hemagglutinin in pre- and postfusion conformations. Here, we present the crystal structure of the secreted, uncleaved ectodomain of the paramyxovirus, human parainfluenza virus 3 fusion (F) protein, a member of the class I viral fusion protein group. The secreted human parainfluenza virus 3 F forms a trimer with distinct head, neck, and stalk regions. Unexpectedly, the structure reveals a six-helix bundle associated with the postfusion form of F, suggesting that the anchor-minus ectodomain adopts a conformation largely similar to the postfusion state. The transmembrane anchor domains of F may therefore profoundly influence the folding energetics that establish and maintain a metastable, prefusion state.
KW - Atomic structure
KW - Class I fusion protein
KW - Membrane fusion
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U2 - 10.1073/pnas.0503989102
DO - 10.1073/pnas.0503989102
M3 - Article
C2 - 15964978
AN - SCOPUS:21544470513
VL - 102
SP - 9288
EP - 9293
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 26
ER -