An engineered allosteric switch in leucine-zipper oligomerization

Nature Structural Biology

Volumn 3, Issue 6, 1996, Pages 510-515

  Gonzalez Jr , Lino ^a   Plecs, Joseph J ^a   Alber, Tom ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LEUCINE ZIPPER PROTEIN;

ALLOSTERISM; ARTICLE; CONFORMATIONAL TRANSITION; HUMAN; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE;

ALLOSTERIC REGULATION; AMINO ACID SEQUENCE; BENZENE; CRYSTALLOGRAPHY, X-RAY; CYCLOHEXANES; DNA-BINDING PROTEINS; ENZYME STABILITY; FUNGAL PROTEINS; LEUCINE ZIPPERS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MUTATION; PROTEIN ENGINEERING; PROTEIN KINASES; PROTEIN STRUCTURE, SECONDARY; SACCHAROMYCES CEREVISIAE PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 0029974730     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0696-510     Document Type: Article

References (14)

1. Bryson, J.W. et al. Protein design: A hierarchic approach. Science 270, 935-941 (1995).
2. Spencer, D.M., Wandless, T.J., Schreiber, S.L. & Crabtree, G.R. Controlling signal transduction with synthetic ligands. Science 262, 1019-1024 (1993).
3. Landschulz, W.H., Johnson, P.F. & McKnight, S.L. The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins. Science 240, 1759-1764 (1988).
4. Peteranderl, R. & Nelson, H.C.M. Trimerization of the heat shock transcription factor by a triple-stranded alpha-helical coiled-coil. Biochemistry 31, 12272-12276 (1992).
5. Parry, D.A.D. & Steinert, P.M. Intermediate filament structure. Curr. Opin. Cell Biol. 4, 94-98 (1992).
6. Hunter, I., Schulthess, T. & Engel, J. Laminin chain assembly by triple and double stranded coiled-coil structures. J. Biol. Chem. 267, 6006-6011 (1992).
7. Kodama, T. et al. Type I macrophage scavenger receptor contains alpha-helical and collagen-like coiled coils. Nature 343, 531-535 (1990).
8. Doi, T. et al. The histidine interruption of an alpha-helical coiled coil allosterically mediates a pH-dependent ligand dissociation from macrophage scavenger receptors. J. Biol. Chem. 269, 25598-25604 (1994).
9. Carr, C.M. & Kim, P.S. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73, 823-832 (1993).
10. Bullough, P.A., Hughson, P.M., Skehel, J.J. & Wiley, D.C. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371, 37-43 (1994).
11. Rabindran, S.K., Haroun, R.I., Clos, J., Wisniewski, J. & Wu, C. Regulation of heat shock factor trimer formation: role of a conserved leucine zipper. Science 259, 230-234 (1993).
12. Oas, T.G. & Endow, S.A. Springs and hinges: dynamic coiled coils and discontinuities. Trends Biochem. Sci. 19, 51-54 (1994)
13. Cohen, C. & Parry, D.A.D. Alpha-helical coiled coils and bundles: how to design an alpha-helical protein. Proteins 7, 1-15 (1990).
14. Harbury, P.B., Kim, P.S. & Alber, T. Crystal structure of an isoleucine-zipper trimer. Nature 371, 80-83 (1994).