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. Acyl-phosphatase (EC 3.6.1.7) w...

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Veröffentlicht in:	FEBS letters 1990-12, Vol.277 (1), p.272-276
Hauptverfasser:	Ghetti, Andrea, Bolognesi, Martino, Cobianchi, Fabio, Morandi, Carlo
Format:	Artikel
Sprache:	eng
Schlagworte:	Acid Anhydride Hydrolases Acylphosphatase Amino Acid Sequence Biological and medical sciences Cell physiology Circular Dichroism Fundamental and applied biological sciences. Psychology Heterogeneous Nuclear Ribonucleoprotein A1 Heterogeneous-Nuclear Ribonucleoprotein Group A-B Heterogeneous-Nuclear Ribonucleoproteins Modeling by homology Models, Molecular Molecular and cellular biology Molecular Sequence Data Phosphoric Monoester Hydrolases - ultrastructure Protein Conformation Ribonucleoproteins - ultrastructure RNA binding domain
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Zusammenfassung:	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. Acyl-phosphatase (EC 3.6.1.7) was selected as template for the modeling experiment. The predicted RNA binding site is a β-sheet containing the two RNP consensus sequences as well as lysines and arginines conserved among the family.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(90)80863-E