Determining the 3D structure of human ASC2 protein involved in apoptosis and inflammation.
ASC2 structure has been well defined by 1141 NOE experimental restraints. The model consists of five alpha helices. alpha-Helices are connected by short random structure loops. The sole exception is the loop connecting helices 2 and 3, which has a 20-residue length. Folding generally agrees with the folding of recently published death domain structures in which alpha-helix structures have been reported. In spite of structural similarity, amino acid sequence homology with the most similar protein (ASC1) is just 64%. DD, DED, and CASP protein structures present six helices along their sequences; ASC2 presents 5 well-defined helices due to long distance restraints. However, a helical fragment was observed between amino acids 38 and 42 (representing helix 3) in the death domains when constructing the model.
Espejo
Fabiola
F
Fundación Instituto de Inmunologia de Colombia (FIDIC). Cra 50 N. 26-00 Bogotá, Colombia. fabiola_espejo@fidic.org
Patarroyo
Manuel E
ME
D027182:Amino Acid Transport System y+ / Q000737:chemistry; D017209:Apoptosis; D051017:Apoptosis Regulatory Proteins / Q000737:chemistry*; D002942:Circular Dichroism; D004926:Escherichia coli / Q000378:metabolism; D006801:Humans; D021621:Imaging, Three-Dimensional / Q000379:methods*; D007249:Inflammation; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010957:Plasmids / Q000378:metabolism; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry; D012261:Ribonucleoproteins / Q000737:chemistry*; D013997:Time Factors; D014466:Ultraviolet Rays
D027182:Amino Acid Transport System y+; D051017:Apoptosis Regulatory Proteins; C490350:POP1 protein, human; D011994:Recombinant Proteins; D012261:Ribonucleoproteins; C498799:SLC7A10 protein, human