The death-effector domain (DED) is a protein interaction domain found in inactive procaspases (cysteine proteases) and proteins that regulate caspase activation in the apoptosis cascade such as FAS-associating death domain-containing protein (FADD). FADD recruits procaspase 8 and procaspase 10 into an death induced signaling complex (DISC). This recruitment is mediated by a homotypic interaction between the procaspase DED and a second DED in an adaptor protein that is directly associated with activated TNF receptors. Complex formation allows proteolytic activation of procaspase into the active caspase form which results in the initiation of apoptosis (cell death). An adaptor protein is a protein which is accessory to main proteins in signal transduction. ... In biology, apoptosis (from the Greek words apo = from and ptosis = falling, pronounced ap-a-tow-sis[1]) is one of the main types of programmed cell death (PCD). ...
BZIP || DED | SH2 | SH3 | Zinc finger Within a protein, a structural domain (domain) is an element of overall structure that is self-stabilizing and often folds independently of the rest of the protein chain. ... Basic Leucine zipper domain (bZIP domain) CREB (top) is a transcription factor capable of binding DNAvia the bZIP domain (bottom) and regulating gene expression. ... An SH3 domain is a protein module, a characteristic peptide sequence. ... A zinc finger is part of a protein that can bind to DNA. Zinc finger domains typically consist of two antiparallel β sheets, each carrying a cysteine residue, and an α helix carrying two histidine residues. ...
Within a protein, a structural domain ("domain") is an element of overall structure that is self-stabilizing and often folds independently of the rest of the protein chain.
Domains often are named and singled out because they figure prominently in the biological function of the protein they belong to; for example, the "calcium-binding" domain of calmodulin.
Given the fact that phosphoinositides are sequestered to various cell membranes (due to their long lipophilic tail) the PH domains usually cause localization of the protein in question to one or another cell membrane, which is useful for expediting activation of the protein and continuation of a signaling pathway.
The SH3domain has a characteristic fold which consists of five or six β-strands arranged as two tightly packed anti-parallel β sheets.
The SH3domain is found in proteins that interact with other proteins and they mediate assembly of specific protein complexes via binding to proline-rich peptides in their respective binding partner.
SH3domains are often found in functions concerning the cytoskeleton, the ras protein, and the src kinase.
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