Proteomics

Dataset Information

0

A heme-binding domain in a voltage gated porassium channel


ABSTRACT: Heme-affinity pull-down assays and proteomics of lysates from primary cortical neurons identified and EAG channel, hERG3 (Kv11.3) binds to heme.

INSTRUMENT(S): Waters instrument model

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Primary Cerebral Cortical Neuron�

SUBMITTER: Rebekah Jukes-Jones  

LAB HEAD: Emma Raven

PROVIDER: PXD019887 | Pride | 2020-09-17

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
TC080907001F002836.mzid.gz Mzid
TC080907001F002836.mzid_TC080907001_F002836.MGF Mzid
TC080907002F002837.mzid.gz Mzid
TC080907002F002837.mzid_TC080907002_F002837.MGF Mzid
TC080907003F002838.mzid.gz Mzid
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Publications


The EAG (<i>ether-à-go-go</i>) family of voltage-gated K<sup>+</sup> channels are important regulators of neuronal and cardiac action potential firing (excitability) and have major roles in human diseases such as epilepsy, schizophrenia, cancer, and sudden cardiac death. A defining feature of EAG (Kv10-12) channels is a highly conserved domain on the N terminus, known as the eag domain, consisting of a Per-ARNT-Sim (PAS) domain capped by a short sequence containing an amphipathic helix (Cap doma  ...[more]

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