期刊
STRUCTURE
卷 16, 期 7, 页码 991-1001出版社
CELL PRESS
DOI: 10.1016/j.str.2008.05.007
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资金
- NIGMS NIH HHS [R01 GM054616] Funding Source: Medline
Single-span transmembrane (TM) helices have structural and functional roles well beyond serving as mere anchors to tether water-soluble domains in the vicinity of the membrane. They frequently direct the assembly of protein complexes and mediate signal transduction in ways analogous to small modular domains in water-soluble proteins. This review highlights different sequence and structural motifs that direct TM assembly and discusses their roles in diverse biological processes. We believe that TM interactions are potential therapeutic targets, as evidenced by natural proteins that modulate other TM interactions and recent developments in the design of TM-targeting peptides.
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