The most significant accomplishment of recent year was the structure solution of the soluble fragment of human TLT-1. We also showed that the soluble variant of this protein exists in vivo, making our finding more relevant. In the process of our efforts while working with TLT-1, we developed the first protocol for expression and folding of the functional preparation of TLT-1 at the preparative scale.

Agency
National Institute of Health (NIH)
Institute
Division of Basic Sciences - NCI (NCI)
Type
Intramural Research (Z01)
Project #
1Z01BC010761-01
Application #
7338827
Study Section
Mammalian Cell Lines Committee (MCL)
Project Start
Project End
Budget Start
Budget End
Support Year
1
Fiscal Year
2006
Total Cost
Indirect Cost
Name
Basic Sciences
Department
Type
DUNS #
City
State
Country
United States
Zip Code
Lubkowski, Jacek; Durbin, Sarah V; Silva, Mariana C C et al. (2017) Structural analysis and unique molecular recognition properties of a Bauhinia forficata lectin that inhibits cancer cell growth. FEBS J 284:429-450
Klusak, Vojtech; Barinka, Cyril; Plechanovova, Anna et al. (2009) Reaction mechanism of glutamate carboxypeptidase II revealed by mutagenesis, X-ray crystallography, and computational methods. Biochemistry 48:4126-38
Barinka, Cyril; Starkova, Jana; Konvalinka, Jan et al. (2007) A high-resolution structure of ligand-free human glutamate carboxypeptidase II. Acta Crystallogr Sect F Struct Biol Cryst Commun 63:150-3
Barinka, Cyril; Rovenska, Miroslava; Mlcochova, Petra et al. (2007) Structural insight into the pharmacophore pocket of human glutamate carboxypeptidase II. J Med Chem 50:3267-73
Barinka, Cyril; Parry, Graham; Callahan, Jennifer et al. (2006) Structural basis of interaction between urokinase-type plasminogen activator and its receptor. J Mol Biol 363:482-95