3bdq
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(New page: 200px<br /><applet load="3bdq" size="350" color="white" frame="true" align="right" spinBox="true" caption="3bdq, resolution 2.000Å" /> '''Room Tempreture Cry...)
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Revision as of 09:20, 23 January 2008
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Room Tempreture Crystal Structure of Sterol Carrier Protein-2 Like-2
Overview
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, 3-dimensional crystal structure of AeSCP-2L2 was solved at 1.7 A, resolution. AeSCP-2L2 forms a dimer and binds 3 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 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 [3H], cholesterol and [3H] palmitic acid. Over-expression of AeSCP-2L2 in, mosquito cells leads to increased uptake of free fatty acid, whereas, knockdown of AeSCP-2L2 in adult females decreases accumulation of free, fatty acid in the fat body from a blood meal. In contrast, over-expression, 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 a dedicated role in cholesterol, transport.
About this Structure
3BDQ is a Single protein structure of sequence from Aedes aegypti with as ligand. Full crystallographic information is available from OCA.
Reference
3-D structure/function analysis of sterol carrier protein-2-like2 reveals differences among SCP-2 family members., Dyer DH, Wessely V, Forest KT, Lan Q, J Lipid Res. 2007 Dec 15;. PMID:18084051
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