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3BDQ

Room Tempreture Crystal Structure of Sterol Carrier Protein-2 Like-2

Summary for 3BDQ
Entry DOI10.2210/pdb3bdq/pdb
Related2QZT
DescriptorSterol carrier protein 2-like 2, PALMITIC ACID (3 entities in total)
Functional Keywordsalpha/beta protein, lipid carrier, sterol carrier protein, lipid transport
Biological sourceAedes aegypti (yellow fever mosquito)
Total number of polymer chains2
Total formula weight24016.22
Authors
Dyer, D.H.,Lan, Q.,Forest, K.T. (deposition date: 2007-11-15, release date: 2008-01-01, 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 (2 Å)
Structure validation

229380

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