quaternary structure

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quaternary structure

n.
The three-dimensional arrangement of the macromolecules making up a functional unit, such as that formed by four globin protein molecules to make hemoglobin or by histones interacting with DNA to make a nucleosome.
References in periodicals archive ?
USH proteins have been shown to interact with one another and form multiprotein complexes and play important roles in the development, maintenance, and function of stereocilia and synapses in the inner ear sensory hair cells [16].
As multiprotein complexes, inflammasomes consist of the effector protein caspase-1, an apoptosis-associated speck-like protein containing a caspase activation and recruitment domain (CARD) (ASC) and a sensor protein from the NOD-like receptor (NLR family) like NLRP1, NLRP3, or absent-in-melanoma (AIM)2 among others [15].
During the past five years, our group has focused on deciphering the mechanisms of multiprotein complexes that mediate mRNA turnover in S.
The NLRP3 inflammasome is the best characterized of these multiprotein complexes; it contains leucine-rich repeats (LRR) in its N-terminal end, a highly conserved central nucleotide-binding domain (NACHT by its acronym, also known as nucleotide oligomerization domain or NOD), and a PYD domain in its C-terminus end (1011).
In mammals, the mTOR catalytic subunit interacts with several proteins to form two big, functionally distinct, multiprotein complexes known as mTORCl (mTOR Complex 1) andmTORC2(mTORComplex2) [7-10] (Figure 1).Complex 1 (mTORC1) is composed of the catalytic subunit mTOR, the regulatory protein Raptor, and the proteins PRAS40, Deptor, and mLST8.
Other factors like Glycyl-L-histidyl-L-lysine (GHK) (Swaim et al., 1996, Canapp et al., 2003), multiprotein complexes containing S100A13 protein (Prudovsky et al., 2003) and Fibronectin, a large extracellular matrix cell adhesion glycoprotein (Ahmed et al., 1999) are known to play additive roles in wound repair mechanism.
Translational control is mediated by the 7-methyl-GTP cap structure present at the 5' termini of all eukaryotic mRNAs where multiprotein complexes are formed during translation initiation.
To answer the true biological questions, researchers need to understand the real 3D, and sometimes 4D, structures of multiprotein complexes; says Gerard Geilen, senior global marketing programs manager at FEI Co., Hillsboro, Ore.
Seminal studies using the fruit fly Drosophila melanogaster in the late 1970s to early 1980s revealed the existence of two large multiprotein complexes with diametrically opposite roles in the regulation of gene expression: the Polycomb group (PcG) and Trithorax group (TrxG) (Lewis 1978; Poux et al.
* Self-assembly of multiprotein complexes IDPs help bring together different proteins to form larger structures--such as the ribosome, a molecular machine that serves as the site of protein synthesis.
Multiprotein complexes (e.g., including components encoded by TINF2 and CTC1) maintain telomeres, and the ribonucleoprotein telomerase [composed of the products of the TERC, TERT, DKC1, TCAB1 (i.e., WRAP53), NHP2, and NOP10 genes] replaces hexanucleotide repeats by reverse transcription to counteract telomere attrition.
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