Fragments of the second transmembrane helix of three G-protein-coupled receptors: comparative synthetic, structural and conformational studies
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DOI: 10.1007/s00726-018-2662-z
Abstract: We compared the synthesis and structural/conformational details of the (66–97) segments of the second transmembrane helix of AT1, MAS and B2, all of which belong to the class of G-protein-coupled receptors (GPCR). Step-by-step monitoring of… read more here.
Keywords: second transmembrane; protein coupled; coupled receptors; transmembrane helix ... See more keywords
Non-canonical Shedding of TNFα by SPPL2a Is Determined by the Conformational Flexibility of Its Transmembrane Helix
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DOI: 10.1016/j.isci.2020.101775
Abstract: Summary Ectodomain (EC) shedding defines the proteolytic removal of a membrane protein EC and acts as an important molecular switch in signaling and other cellular processes. Using tumor necrosis factor (TNF)α as a model substrate,… read more here.
Keywords: tnf; canonical shedding; sppl2a; non canonical ... See more keywords
Importance of transmembrane helix 4 of l-alanine exporter AlaE in oligomer formation and substrate export activity in Escherichia coli.
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DOI: 10.1099/mic.0.001147
Abstract: AlaE is the smallest amino acid exporter identified in Escherichia coli. It exports l-alanine using the proton motive force and plays a pivotal role in maintaining intracellular l-alanine homeostasis by acting as a safety valve.… read more here.
Keywords: escherichia coli; transmembrane helix; gxxxg motif; activity ... See more keywords
Structure of the GOLD-domain seven-transmembrane helix protein family member TMEM87A
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DOI: 10.1101/2022.06.20.496907
Abstract: TMEM87s are eukaryotic transmembrane proteins with two members (TMEM87A and TMEM87B) in humans. TMEM87s have proposed roles in protein transport to and from the Golgi, as mechanosensitive ion channels, and in developmental signaling. TMEM87 disruption… read more here.
Keywords: tmem87a; transmembrane helix; domain; seven transmembrane ... See more keywords
The transmembrane α‐helix of LptC participates in LPS extraction by the LptB2FGC transporter
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DOI: 10.1111/mmi.14952
Abstract: Lipopolysaccharide (LPS) is an essential component of the outer membrane of most Gram‐negative bacteria that provides resistance to various toxic compounds and antibiotics. Newly synthesized LPS is extracted from the inner membrane by the ATP‐binding… read more here.
Keywords: transporter; transmembrane helix; lptc participates; lptb2fgc ... See more keywords