1b5l
From Proteopedia
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OVINE INTERFERON TAU
Overview
Ovine interferon-tau (ovIFN-tau) is a pregnancy recognition hormone, required for normal embryonic development in sheep. In addition to its, novel role in reproductive physiology, ovIFN-tau displays antiviral and, antiproliferative activities similar to the IFN-alpha subtypes. To probe, the structural basis for its unique activity profile, the crystal, structure of ovIFN-tau has been determined at 2.1 A resolution. The fold, of ovIFN-tau is similar to the previously determined crystal structures of, human IFN-alpha2b and human and murine IFN-beta, which each contain five, alpha-helices. Comparison of ovIFN-tau with huIFN-alpha2b, huIFN-beta, and, muIFN-beta reveals unexpected structural differences that occur in regions, of considerable sequence identity. Specifically, main-chain differences up, to 11 A occur for residues in helix A, the AB loop, helix B, and the BC, loop. Furthermore, these regions are known to be important for receptor, binding and biological activity. Of particular interest, a buried ion pair, is observed in ovIFN-tau between Glu71 and Arg145 which displaces a, conserved tryptophan residue (Trp77) from the helical bundle core. This, ion pair represents a major change in the core of ovIFN-tau compared to, huIFN-alpha2b. Based on amino acid sequence comparisons, these ovIFN-tau, structural features may be conserved in several human IFN-alpha subtypes, and IFN-omega. The structure identifies potential problems in interpreting, site-directed mutagenesis data on the human IFN-alpha family that consists, of 12 proteins.
About this Structure
1B5L is a Single protein structure of sequence from Pichia pastoris with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of ovine interferon-tau at 2.1 A resolution., Radhakrishnan R, Walter LJ, Subramaniam PS, Johnson HM, Walter MR, J Mol Biol. 1999 Feb 12;286(1):151-62. PMID:9931256
Page seeded by OCA on Tue Nov 20 11:22:54 2007
