The Protein Expression core will assist various components of the program project in the production of proteins and complexes of proteins to be studied by X-ray crystallography and NMR. Specifically, this facility will scale up expression and purification of native proteins and protein fragments initially generated by individual scale. It will also maintain and provide cells and expression vectors for large-scale production. The core will provide advice and support to all members of all projects, regarding standard procedures and methods used for protein expression and purification.

Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Research Program Projects (P01)
Project #
5P01HL048675-10
Application #
6657107
Study Section
Heart, Lung, and Blood Initial Review Group (HLBP)
Project Start
2002-09-01
Project End
2003-08-31
Budget Start
Budget End
Support Year
10
Fiscal Year
2002
Total Cost
$310,486
Indirect Cost
Name
Immune Disease Institute, Inc.
Department
Type
DUNS #
115524410
City
Boston
State
MA
Country
United States
Zip Code
02115
Finci, L; Zhang, Y; Meijers, R et al. (2015) Signaling mechanism of the netrin-1 receptor DCC in axon guidance. Prog Biophys Mol Biol 118:153-60
Jiang, Jian-kang; McCoy, Joshua G; Shen, Min et al. (2014) A novel class of ion displacement ligands as antagonists of the ?IIb?3 receptor that limit conformational reorganization of the receptor. Bioorg Med Chem Lett 24:1148-53
Liu, Ying; Zhang, Yan; Wang, Jia-Huai (2014) Crystal structure of human Ankyrin G death domain. Proteins 82:3476-82
Finci, Lorenzo I; Krüger, Nina; Sun, Xiaqin et al. (2014) The crystal structure of netrin-1 in complex with DCC reveals the bifunctionality of netrin-1 as a guidance cue. Neuron 83:839-849
Chen, Qiang; Sun, Xiaqin; Zhou, Xiao-hong et al. (2013) N-terminal horseshoe conformation of DCC is functionally required for axon guidance and might be shared by other neural receptors. J Cell Sci 126:186-95
Wang, Jia-Huai (2013) The sequence signature of an Ig-fold. Protein Cell 4:569-72
Xu, Amy J; Springer, Timothy A (2013) Mechanisms by which von Willebrand disease mutations destabilize the A2 domain. J Biol Chem 288:6317-24
Wang, Jia-huai; Reinherz, Ellis L (2012) The structural basis of ?? T-lineage immune recognition: TCR docking topologies, mechanotransduction, and co-receptor function. Immunol Rev 250:102-19
Yu, Yamei; Zhu, Jianghai; Mi, Li-Zhi et al. (2012) Structural specializations of ?(4)?(7), an integrin that mediates rolling adhesion. J Cell Biol 196:131-46
Xu, Amy J; Springer, Timothy A (2012) Calcium stabilizes the von Willebrand factor A2 domain by promoting refolding. Proc Natl Acad Sci U S A 109:3742-7

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