Solution Structure of Peptide Toxins That Block Mechanosensitive Ion Channels
نویسندگان
چکیده
منابع مشابه
Solution structure of peptide toxins that block mechanosensitive ion channels.
Mechanosensitive channels (MSCs) play key roles in sensory processing and have been implicated as primary transducers for a variety of cellular responses ranging from osmosensing to gene expression. This paper presents the first structures of any kind known to interact specifically with MSCs. GsMTx-4 and GsMtx-2 are inhibitor cysteine knot peptides isolated from venom of the tarantula, Grammost...
متن کاملMechanosensitive ion channels
Cell surface receptors are involved in numerous important biological processes including embryogenesis, tissue differentiation, and cellular homeostasis. Among them, mechanosensitive ion channels play an essential role in cellular functions of every cell including neurons, cardiomyocytes, and osteocytes. Here, we discuss types, roles, structures, and biophysical factors that affect the function...
متن کاملMechanosensitive ion channels
Mechanosensitive (MS) ion channels are to date the best characterized biological force-sensing systems. They present the best example of coupling protein conformations to the mechanics of the surrounding cell membrane. Studies of MS channels conducted over the last 28 years have from their serendipitous discovery and confusion about their artifactual nature to their molecular identification and...
متن کاملBlock of voltage-gated calcium channels by peptide toxins.
Venoms from various predatory species, such as fish hunting molluscs scorpions, snakes and arachnids contain a large spectrum of toxins that include blockers of voltage-gated calcium channels. These peptide blockers act by two principal manners - physical occlusion of the pore and prevention of activation gating. Many of the calcium channel-blocking peptides have evolved to tightly occupy their...
متن کاملGsMTx4: Mechanism of Inhibiting Mechanosensitive Ion Channels.
GsMTx4 is a spider venom peptide that inhibits cationic mechanosensitive channels (MSCs). It has six lysine residues that have been proposed to affect membrane binding. We synthesized six analogs with single lysine-to-glutamate substitutions and tested them against Piezo1 channels in outside-out patches and independently measured lipid binding. Four analogs had ∼20% lower efficacy than the wild...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2002
ISSN: 0021-9258
DOI: 10.1074/jbc.m202715200