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Science 24 December 1993:
Vol. 262. no. 5142, pp. 2027 - 2030
DOI: 10.1126/science.8266097
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Articles

Science, Vol 262, Issue 5142, 2027-2030
Copyright © 1993 by American Association for the Advancement of Science

articles

Crystal structure of the repetitive segments of spectrin

Y Yan, E Winograd, A Viel, T Cronin, SC Harrison, and D Branton

Department of Biochemistry, Harvard University, Cambridge, MA 02138.

The elongated proteins of the spectrin family (dystrophin, alpha-actinin, and spectrin) contain tandemly repeated segments and form resilient cellular meshworks by cross-linking actin filaments. The structure of one of the repetitive segments of alpha-spectrin was determined at a 1.8 angstrom resolution. A segment consists of a three-helix bundle. A model of the interface between two tandem segments suggests that hydrophobic interactions between segments may constrain intersegment flexibility. The helix side chain interactions explain how mutations that are known to produce hemolytic anemias disrupt spectrin associations that sustain the integrity of the erythrocyte membrane.


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Dynamic molecular modeling of pathogenic mutations in the spectrin self-association domain.
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Interactions of the alpha -Spectrin N-terminal Region with beta -Spectrin. IMPLICATIONS FOR THE SPECTRIN TETRAMERIZATION REACTION.
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Engineering a Lever into the Kinesin Neck.
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A Cluster of Basic Repeats in the Dystrophin Rod Domain Binds F-actin through an Electrostatic Interaction.
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Spectrin St Claude, a Splicing Mutation of the Human alpha -Spectrin Gene Associated With Severe Poikilocytic Anemia.
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Characterization of the interactions of alpha-catenin with alpha-actinin and beta-catenin/plakoglobin.
J. Nieset, A. Redfield, F Jin, K. Knudsen, K. Johnson, and M. Wheelock (1997)
J. Cell Sci. 110, 1013-1022
   Abstract »    PDF »
Peptides with More than One 106-amino Acid Sequence Motif Are Needed to Mimic the Structural Stability of Spectrin.
N. Menhart, T. Mitchell, D. Lusitani, N. Topouzian, and L. W.-M. Fung (1996)
J. Biol. Chem. 271, 30410-30416
   Abstract »    Full Text »    PDF »
Identification of the Spectrin Subunit and Domains Required for Formation of Spectrin/Adducin/Actin Complexes.
X. Li and V. Bennett (1996)
J. Biol. Chem. 271, 15695-15702
   Abstract »    Full Text »    PDF »
Mapping the Human Erythrocyte beta-Spectrin Dimer Initiation Site Using Recombinant Peptides and Correlation of Its Phasing with the alpha-Actinin Dimer Site.
J. A. Ursitti, L. Kotula, T. M. DeSilva, P. J. Curtis, and D. W. Speicher (1996)
J. Biol. Chem. 271, 6636-6644
   Abstract »    Full Text »    PDF »
Alpha-helical coiled coils: more facts and better predictions.
C Cohen and D. Parry (1994)
Science 263, 488-489
   PDF »
Identification and Characterization of beta V Spectrin, a Mammalian Ortholog of Drosophilabeta H Spectrin.
P. R. Stabach and J. S. Morrow (2000)
J. Biol. Chem. 275, 21385-21395
   Abstract »    Full Text »    PDF »
Isoforms of Kalirin, a Neuronal Dbl Family Member, Generated through Use of Different 5'- and 3'-Ends Along with an Internal Translational Initiation Site.
R. C. Johnson, P. Penzes, B. A. Eipper, and R. E. Mains (2000)
J. Biol. Chem. 275, 19324-19333
   Abstract »    Full Text »    PDF »
Syne-1, A Dystrophin- and Klarsicht-related Protein Associated with Synaptic Nuclei at the Neuromuscular Junction.
E. D. Apel, R. M. Lewis, R. M. Grady, and J. R. Sanes (2000)
J. Biol. Chem. 275, 31986-31995
   Abstract »    Full Text »    PDF »
A New Spectrin, beta IV, Has a Major Truncated Isoform That Associates with Promyelocytic Leukemia Protein Nuclear Bodies and the Nuclear Matrix.
W. T. Tse, J. Tang, O. Jin, C. Korsgren, K. M. John, A. L. Kung, B. Gwynn, L. L. Peters, and S. E. Lux (2001)
J. Biol. Chem. 276, 23974-23985
   Abstract »    Full Text »    PDF »
Folding Intermediates of a Model Three-helix Bundle Protein. PRESSURE AND COLD DENATURATION STUDIES.
A. Chapeaurouge, J. S. Johansson, and S. T. Ferreira (2001)
J. Biol. Chem. 276, 14861-14866
   Abstract »    Full Text »    PDF »


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