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2QZT

Crystal Structure of Sterol Carrier Protein 2 Like 2 (SCP2-L2) from Aedes Aegypti

Summary for 2QZT
Entry DOI10.2210/pdb2qzt/pdb
Related1PZ4
DescriptorSterol carrier protein 2-like 2, PALMITIC ACID (3 entities in total)
Functional Keywordssterol carrier, mosquito, fatty acid, palmitic acid, cholesterol, lipid transport
Biological sourceAedes aegypti (yellow fever mosquito)
Total number of polymer chains2
Total formula weight24130.32
Authors
Dyer, D.H.,Lan, Q.,Forest, K.T. (deposition date: 2007-08-17, release date: 2008-03-11, Last modification date: 2024-02-21)
Primary citationDyer, D.H.,Wessely, V.,Forest, K.T.,Lan, Q.
Three-dimensional structure/function analysis of SCP-2-like2 reveals differences among SCP-2 family members.
J.Lipid Res., 49:644-653, 2008
Cited by
PubMed Abstract: Mosquito sterol carrier protein-2 (AeSCP-2) and sterol carrier protein-2-like2 (AeSCP-2L2) are members of the SCP-2 protein family with similar expression profiles in the mosquito life cycle. In an effort to understand how lipids can be transported by different SCP-2 proteins, the three-dimensional crystal structure of AeSCP-2L2 was solved at 1.7 A resolution. AeSCP-2L2 forms a dimer and binds three fatty acids, one of which resides in a position within the internal cavity at a right angle to the others. This first report of ligand-bound dimerized protein in the SCP-2 protein family indicates that the family has a much more divergent mode of interaction with ligands than previously reported. The potential function of AeSCP-2L2 was investigated via in vivo incorporation of [(3)H]cholesterol and [3H]palmitic acid. Overexpression of AeSCP-2L2 in mosquito cells leads to an increased uptake of free fatty acid, whereas knockdown of AeSCP-2L2 in adult females decreases the accumulation of free fatty acid in the fat body from a blood meal. In contrast, overexpression or knockdown of AeSCP-2L2 has no effect on cholesterol uptake. Our results suggest that the main function of AeSCP-2L2 is as a general intracellular fatty acid carrier, as opposed to having a dedicated role in cholesterol transport.
PubMed: 18084051
DOI: 10.1194/jlr.M700460-JLR200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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