Modeling by homology of RNA binding domain in A1 hnRNP protein.
Eukaryotic nuclear RNA binding proteins share a common sequence motif thought to be implicated in RNA binding. One of the two domains present in A1 hnRNP protein, has been modelled by homology in order to make a prediction of the main features of the RNA binding site. Acylphosphatase (EC 3.6.1.7) was selected as template for the modeling experiment. The predicted RNA binding site is a beta-sheet containing the two RNP consensus sequences as well as lysines and arginines conserved among the family.
Ghetti
A
A
Instituto di Scienze Biologiche, Università di Verona, Italy.
Bolognesi
M
M
Cobianchi
F
F
Morandi
C
C
D017766:Acid Anhydride Hydrolases; D000595:Amino Acid Sequence; D002942:Circular Dichroism; D000076245:Heterogeneous Nuclear Ribonucleoprotein A1; D034481:Heterogeneous-Nuclear Ribonucleoprotein Group A-B; D034441:Heterogeneous-Nuclear Ribonucleoproteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010744:Phosphoric Monoester Hydrolases / Q000648:ultrastructure; D011487:Protein Conformation; D012261:Ribonucleoproteins / Q000648:ultrastructure*; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D000076245:Heterogeneous Nuclear Ribonucleoprotein A1; D034481:Heterogeneous-Nuclear Ribonucleoprotein Group A-B; D034441:Heterogeneous-Nuclear Ribonucleoproteins; D010744:Phosphoric Monoester Hydrolases; D012261:Ribonucleoproteins; D000097024:Acylphosphatase