ISSN:
0887-3585
Schlagwort(e):
α interferon
;
β interferon
;
homology modeling
;
Chemistry
;
Biochemistry and Biotechnology
Quelle:
Wiley InterScience Backfile Collection 1832-2000
Thema:
Medizin
Notizen:
An atomic coordinate five α-helix three-dimensional model is presented for human interferon α-2 (HuIFNα2). The HuIFNα2 structure was constructed from murine interferon β (MuIFNβ) by homology modeling using the STEREO and IMPACT programs. The HuIFNα2 model is consistent with its known biochemical and biophysical properties including epitope mapping. Lysine residues predicted to be buried in the model were primarily unreactive with succinimidyl-7-amino-4-methylcoumarin-3-acetic acid (AMCA-NHS), a lysine modification agent, as shown by mass spectrometric analysis of tryptic digests. N-terminal sequence analysis of polypeptides generated by limited digestion of HuIFNα2 with endoproteinase Lys-C demonstrated rapid cleavage at K31, which is consistent with the presence of this residue in a loop in the proposed HuIFNα2 model. Based on this model structure potential receptor binding sites are identified. © 1993 Wiley-Liss, Inc.
Zusätzliches Material:
3 Ill.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1002/prot.340170109
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