Document Detail


A three-dimensional model of interferon-tau.
MedLine Citation:
PMID:  8746786     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The interferon-tau (IFN-tau) are type I IFN whose expression is restricted to the embryonic trophectoderm of the developing placenta of ruminant ungulate species, where they act as hormones of pregnancy. Here computer modeling has been used to generate homology models of bovine and ovine IFN-tau based on the refined crystal structure of murine IFN-beta. The IFN-tau structure, like that of MuIFN-beta, is based on five long alpha helices (A-E), one short helix in the middle of the loop connecting helices C and D and a long loop between helices A and B. BoIFN-tau differs from MuIFN-beta in three important respects. First, as in all IFN-tau, there is a carboxyl tail of nine amino acids that cannot be accurately modeled but that would have a length of approximately 30 A when fully extended. Second, like the IFN-alpha subtype, all IFN-tau have a three-amino acid insertion in loop AB and a likely disulfide bridge between Cys29 and Cys139 that lead to marked conformational differences between them and MuIFN-beta in a region (Leu22 to Arg33 in IFN-tau) believed to interact with the receptor. Third, all IFN-tau, as well as the related IFN-omega, possess a Gly at position 126 (rather than the equivalent Arg on MuIFN-beta and IFN-alpha) that will impair an extensive hydrogen bonding interaction between helix D and loop AB. As a result, the polypeptide segment around this region (Phe36 to Gln40) of loop AB is likely to be considerably more flexible than in other type I IFN.
Authors:
T Senda; S I Saitoh; Y Mitsui; J Li; R M Roberts
Related Documents :
12396726 - Cytotoxicity of combinations of ifn-beta and chemotherapeutic drugs.
6498826 - Relative contribution of antiproliferative and host immunity-associated activity of mou...
8082716 - Association of protein disulfide isomerase activity and the induction of contact inhibi...
25387356 - Human serum albumin-trail conjugate for the treatment of rheumatoid arthritis.
18700156 - Dextrin-rhegf conjugates as bioresponsive nanomedicines for wound repair.
19789446 - Toll-like receptor 4 mediates neutrophil sequestration and lung injury induced by endot...
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research     Volume:  15     ISSN:  1079-9907     ISO Abbreviation:  J. Interferon Cytokine Res.     Publication Date:  1995 Dec 
Date Detail:
Created Date:  1997-02-12     Completed Date:  1997-02-12     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  9507088     Medline TA:  J Interferon Cytokine Res     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1053-60     Citation Subset:  IM    
Affiliation:
Department of BioEngineering, Nagaoka University of Technology, Niigata, Japan.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Computer Simulation*
Crystallography
Humans
Models, Molecular*
Molecular Sequence Data
Protein Structure, Secondary*
Receptors, Interferon / chemistry*
Sequence Homology, Amino Acid
Species Specificity
Grant Support
ID/Acronym/Agency:
HD21896/HD/NICHD NIH HHS
Chemical
Reg. No./Substance:
0/Receptors, Interferon; 0/interferon tau receptor

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


Previous Document:  Potential application of human interferon-alpha in microbial infections of the oral cavity.
Next Document:  Serum interleukin-6 levels in the steady state of sickle cell disease.