This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3bdq
From Proteopedia
(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...) |
|||
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | Mosquito sterol carrier protein-2 (AeSCP-2) and sterol carrier | + | 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 [(3)H]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. |
==About this Structure== | ==About this Structure== | ||
| Line 10: | Line 10: | ||
==Reference== | ==Reference== | ||
| - | + | Three-dimensional structure/function analysis of SCP-2-like2 reveals differences among SCP-2 family members., Dyer DH, Wessely V, Forest KT, Lan Q, J Lipid Res. 2008 Mar;49(3):644-53. Epub 2007 Dec 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18084051 18084051] | |
[[Category: Aedes aegypti]] | [[Category: Aedes aegypti]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dyer, D | + | [[Category: Dyer, D H.]] |
| - | [[Category: Forest, K | + | [[Category: Forest, K T.]] |
[[Category: Lan, Q.]] | [[Category: Lan, Q.]] | ||
[[Category: PLM]] | [[Category: PLM]] | ||
| Line 22: | Line 22: | ||
[[Category: sterol carrier protein]] | [[Category: sterol carrier protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:05:01 2008'' |
Revision as of 17:05, 21 February 2008
|
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 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 [(3)H]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.
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
Three-dimensional structure/function analysis of SCP-2-like2 reveals differences among SCP-2 family members., Dyer DH, Wessely V, Forest KT, Lan Q, J Lipid Res. 2008 Mar;49(3):644-53. Epub 2007 Dec 15. PMID:18084051
Page seeded by OCA on Thu Feb 21 19:05:01 2008
