Proteolipid in the context of Role of chance in scientific discoveries


Proteolipid in the context of Role of chance in scientific discoveries

⭐ Core Definition: Proteolipid

A proteolipid is a protein covalently linked to lipid molecules, which can be fatty acids, isoprenoids or sterols. The process of such a linkage is known as protein lipidation, and falls into the wider category of acylation and post-translational modification. Proteolipids are abundant in brain tissue, and are also present in many other animal and plant tissues. They include ghrelin, a peptide hormone associated with feeding. Many proteolipids have bound fatty acid chains, which often provide an interface for interacting with biological membranes and act as lipidons that direct proteins to specific zones.

Proteolipids were discovered serendipitously in 1951 by Jordi Folch Pi and Marjorie Lees while extracting sulfatides from brain lipids.

↓ Menu
HINT:

In this Dossier

Proteolipid in the context of Protomer (structural biology)

In structural biology, a protomer is the structural unit of an oligomeric protein. It is the smallest unit composed of at least one protein chain. The protomers associate to form a larger oligomer of two or more copies of this unit. Protomers usually arrange in cyclic symmetry to form closed point group symmetries.

The term was introduced by Chetverin to make nomenclature in the Na/K-ATPase enzyme unambiguous. This enzyme is composed of two subunits: a large, catalytic α subunit, and a smaller glycoprotein β subunit (plus a proteolipid, called γ-subunit). At the time it was unclear how many of each work together. In addition, when people spoke of a dimer, it was unclear whether they were referring to αβ or to (αβ)2. Chetverin suggested to call αβ a protomer and (αβ)2 a diprotomer. Thus, in the work by Chetverin the term protomer was only applied to a hetero-oligomer and subsequently used mainly in the context of hetero-oligomers. Following this usage, a protomer consists of a least two different proteins chains. In current literature of structural biology, the term is commonly also applied to the smallest unit of homo-oligomers, avoiding the term "monomer".

View the full Wikipedia page for Protomer (structural biology)
↑ Return to Menu

Proteolipid in the context of Lipidation

Lipid-anchored proteins (also known as lipid-linked proteins) are proteins that are covalently attached to lipids embedded into biological membranes. The lipid-anchored protein can be located on either side of the cell membrane. Thus, the lipid serves to anchor the protein to the cell membrane. Such proteins are a type of proteolipids.

The lipid groups contribute to the intracellular localization and the biological function of the protein to which they are attached. The lipid serves as a mediator of the protein association with specific biological membranes and protein-protein interactions. The lipidation can also sequester a protein away from its substrate to inactivate the protein and then activate it by substrate presentation.

View the full Wikipedia page for Lipidation
↑ Return to Menu