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Titolo:
PREDICTED STRUCTURAL MOTIF OF IFN-TAU
Autore:
JARPE MA; JOHNSON HM; BAZER FW; OTT TL; CURTO EV; KRISHNA NR; PONTZER CH;
Indirizzi:
CAMBRIDGE NEUROSCI INC CAMBRIDGE MA 02139 UNIV ALABAMA,DEPT PHYSIOL & BIOPHYS BIRMINGHAM AL 35294 UNIV FLORIDA,DEPT MICROBIOL & CELL SCI GAINESVILLE FL 32611 TEXAS A&M UNIV,DEPT ANIM SCI COLLEGE STN TX 77843 UNIV ALABAMA,CTR COMPREHENS CANC BIRMINGHAM AL 35294 UNIV ALABAMA,DEPT BIOCHEM BIRMINGHAM AL 35294 UNIV MARYLAND,DEPT MICROBIOL COLLEGE PK MD 20742
Titolo Testata:
Protein engineering
fascicolo: 7, volume: 7, anno: 1994,
pagine: 863 - 867
SICI:
0269-2139(1994)7:7<863:PSMOI>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
OVINE TROPHOBLAST PROTEIN-1; 3-DIMENSIONAL SOLUTION STRUCTURE; PREGNANCY RECOGNITION HORMONE; CRYSTAL-STRUCTURE; MAGNETIC-RESONANCE; ANTIVIRAL ACTIVITY; DISTANCE GEOMETRY; INTERFERON-GAMMA; SEQUENCE; HOMOLOGY;
Keywords:
IFN-TAU; INTERFERON; OVINE TROPHOBLAST PROTEIN-1; PREDICTED STRUCTURE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
31
Recensione:
Indirizzi per estratti:
Citazione:
M.A. Jarpe et al., "PREDICTED STRUCTURAL MOTIF OF IFN-TAU", Protein engineering, 7(7), 1994, pp. 863-867

Abstract

Ovine interferon tau (TFN tau) is a type I interferon that,vas originally identified as ovine trophoblast protein and is associated with the maternal recognition of pregnancy in sheep. Additionally, IFN tau possesses potent antiviral and antiproliferative activity without the corresponding toxicity found in known IFN alpha s. Structure-function studies with synthetic peptides have identified three discontinuous functional sites on the protein that are involved in receptor interaction and biological activity. However, the structural relationship of theseregions is unknown. Therefore, a model of the 3-D structure of IFN tau would be useful in interpretation of existing data and the design offuture structure-function studies. Combining information from circular dichroism (CD) of both the full length recombinant IFN tau and synthetic peptides representing regions of the IFN tau molecule, with sequence homology of IFN tau to IFN beta, a protein of known 3-D structure,we have constructed a model of IFN tau using distance geometry and energy minimization methods. The most striking feature of this model is that functionally active domains of IFN tau, discontinuous in the primary structure, are localized to one side of the molecule and found to be spatially contiguous. This observation is consistent with multiple binding sites on IFN tau interacting simultaneously with the IFN tau receptor.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/10/20 alle ore 08:14:57