Structural basis of neuronal ceroid lipofuscinosis 1

Brain and Development

Volumn 32, Issue 7, 2010, Pages 524-530

  Ohno, Kazuki ^a   Saito, Seiji ^b   Sugawara, Kanako ^c   Suzuki, Toshihiro ^c   Togawa, Tadayasu ^c   Sakuraba, Hitoshi ^c  

^a NPO for the Promotion of Research on Intellectual Property Tokyo   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c MEIJI PHARMACEUTICAL UNIVERSITY   (Japan)

Author keywords

Neuronal ceroid lipofuscinosis 1; Palmitoyl protein thioesterase 1; Protein structure

Indexed keywords

ALANINE; AMINO ACID; ARGININE; ASPARTIC ACID; GLUTAMIC ACID; GLUTAMINE; GLYCINE; LYSINE; METHIONINE; PALMITOYL PROTEIN THIOESTERASE; TRYPTOPHAN; TYROSINE; VALINE; MEMBRANE PROTEIN; PPT1 PROTEIN, HUMAN;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME LOCALIZATION; ENZYME STRUCTURE; HUMAN; NEURONAL CEROID LIPOFUSCINOSIS; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS; ANIMAL; BOVINAE; CHEMICAL STRUCTURE; CHEMISTRY; COMPUTER PROGRAM; ENZYMOLOGY; GENETICS;

AMINO ACID SUBSTITUTION; ANIMALS; CATTLE; HUMANS; MEMBRANE PROTEINS; MODELS, MOLECULAR; NEURONAL CEROID-LIPOFUSCINOSES; SOFTWARE;

EID: 77954385491     PISSN: 03877604     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.braindev.2009.08.010     Document Type: Article

References (12)

1. Camp L., Verkruyse L., Afendis S., Slaughter C., Hofmann S. Molecular cloning and expression of palmitoyl-protein thioesterase. J Biol Chem 1994, 269:23212-23219.
2. Schriner L., Yi W., Hofmann S. CDNA and genomic cloning of human palmitoyl-protein thioesterase (PPT), the enzyme defective in infantile neuronal ceroid lipofuscinosis. Genomics 1996, 34:317-322.
3. NCL Resource. Available from: http://www.ucl.ac.uk/ncl/cln1.shtml.
4. Das A., Lu J., Hofmann S. Biochemical analysis of mutations in palmitoyl-protein thioesterase causing infantile and late-onset forms of neuronal ceroid lipofuscinosis. Hum Mol Genet 2001, 10:1431-1439.
5. Bellizzi J., Widom J., Kemp C., Lu J., Das A., Hofmann S., et al. The crystal structure of palmitoyl protein thioesterase 1 and the molecular basis of infantile neuronal ceroid lipofuscinosis. Proc Natl Acad Sci USA 2000, 97:4573-4578.
6. Petrey D., Xiang X., Tang C., Xie L., Gimpelev M., Mitors T., et al. Using multiple structure alignments, fast model building, and energetic analysis in fold recognition and homology modeling. Protein Struc Func Genet 2003, 53:430-435.
7. Kundrot C., Ponder J., Richards F. Algorithms for calculating excluded volume and its derivatives as a function of molecular conformation and their use in energy minimization. J Comp Chem 1991, 12:402-409.
8. Dudek M., Ponder J. Accurate modeling of the intramolecular electrostatic energy of proteins. J Comput Chem 1995, 16:791-816.
9. Kabsch W. A discussion of the solution for the best rotation to relate two sets of vectors. Acta Cryst 1978, A34:922-923.
10. Matsuzawa F., Aikawa S., Doi H., Okumiya T., Sakuraba H. Fabry disease: correlation between structural changes in α-galactosidase, and clinical and biochemical phenotypes. Hum Genet 2005, 117:317-328.
11. Ahmad S., Gromiha M., Fawareh H., Sarai A. ASAView: Database and tool for solvent accessibility representation in proteins. BMC Bioinformatics 2004, 5:51.
12. McDonald I., Thornton J. Satisfying hydrogen bonding potential in proteins. J Mol Biol 1994, 238:777-793.