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A homology model of human interferon α‐2
Author(s) -
Murgolo Nicholas J.,
Windsor William T.,
Hruza Alan,
Reichert Paul,
Tsarbopoulos Anthony,
Baldwin Samuel,
Huang Eric,
Pramanik Birendra,
Ealick Steven,
Trotta Paul P.
Publication year - 1993
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340170109
Subject(s) - homology modeling , alpha interferon , chemistry , lysine , cleavage (geology) , amino acid , epitope , peptide sequence , homology (biology) , alpha (finance) , peptide , interferon , stereochemistry , acetic acid , binding site , amino acid residue , biochemistry , biology , antibody , enzyme , virology , genetics , medicine , gene , patient satisfaction , paleontology , fracture (geology) , construct validity , nursing
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.