2hie

An atomic coordinate five alpha-helix three-dimensional model is presented for human interferon alpha-2 (HuIFN alpha 2). The HuIFN alpha 2 structure was constructed from murine interferon beta (MuIFN beta) by homology modeling using the STEREO and IMPACT programs. The HuIFN alpha 2 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 HuIFN alpha 2 with endoproteinase Lys-C demonstrated rapid cleavage at K31, which is consistent with the presence of this residue in a loop in the proposed HuIFN alpha 2 model. Based on this model structure potential receptor binding sites are identified.

A homology model of human interferon alpha-2., Murgolo NJ, Windsor WT, Hruza A, Reichert P, Tsarbopoulos A, Baldwin S, Huang E, Pramanik B, Ealick S, Trotta PP, Proteins. 1993 Sep;17(1):62-74. PMID:8234245

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Categories: Ealick, S | Hruza, A | Murgolo, N J | Reichert, P | Trotta, P P | Windsor, W T