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Function
Apolipoproteins are proteins that coat lipoprotein surface that binds lipids such as cholesterol, low-density lipoprotein (LDL), or high-density lipoproteins (HDL) in lipid metabolism. They function in the transport of such lipids in their structure that acts as a ligand to cell receptors and lipid transport proteins. Amphipathic structural behavior are what allows the interaction between hydrophobic properties of water, such as in the blood stream and hydrophobic lipids.
Apolipoprotein A-I is a protein APOA1 gene in humans that is a component of HDL, which a form of good cholesterol in human's diet, used in the transport of cholesterol and phospholipids in the body through the bloodstream in the reverse transport of cholesterol from the tissues to the liver of hepatocytes. They promote cholesterol efflux, a pathway in transferring intracellular cholesterol to extracellular acceptors, from tissues and act as a cofactor for the lecithin cholesterol acyltransferase (LCAT).
Structure
Apolipoprotein a-1 (apoA-I) is a fairly small molecule that consists of a total of 243 residues and is 29-kD polypeptide in size. Structure in color is shown in rainbow, in arrangement from N-terminus (red) of amine group to C-terminus (dark blue) end of carboxyl group. Its structure reveals a N-terminal with four helix bundle and 2 helices at C terminal. N terminal is important maintaining a lipid-free conformation, while C terminus ( 190-243 residues/scene>domain plays key role in lipid binding.
== Clinical significance ==
== Diesease ==
== Structural highlights ==
Apolipoprotein a-1 in the monomer form truncated (lacking 1-43 residues) consists of unique pseudo-continuous alpha helix highlighted by kinks at <scene name='75/752268/Truncated/3'>Pro residues, spaced approximately every 22 residues.
This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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