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Literature DB >> 8266097

Crystal structure of the repetitive segments of spectrin.

Y Yan¹, E Winograd, A Viel, T Cronin, S C Harrison, D Branton.

Abstract

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.

Entities: Disease Gene

Mesh：

Substances：
Spectrin

Year: 1993 PMID： 8266097 DOI： 10.1126/science.8266097

Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728

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Cited

105 in total

8. Separating the effects of internal friction and transition state energy to explain the slow, frustrated folding of spectrin domains.

Authors: Beth G Wensley; Lee Gyan Kwa; Sarah L Shammas; Joseph M Rogers; Stuart Browning; Ziqi Yang; Jane Clarke
Journal: Proc Natl Acad Sci U S A Date: 2012-06-18 Impact factor: 11.205

Review 9. The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life.

Authors: Anthony J Baines
Journal: Protoplasma Date: 2010-07-29 Impact factor: 3.356

10. Structural and dynamic study of the tetramerization region of non-erythroid alpha-spectrin: a frayed helix revealed by site-directed spin labeling electron paramagnetic resonance.

Authors: Qufei Li; L W-M Fung
Journal: Biochemistry Date: 2009-01-13 Impact factor: 3.162

Crystal structure of the repetitive segments of spectrin.

1. Alpha actinin-CapZ, an anchoring complex for thin filaments in Z-line.

2. Flexibility of the alpha-spectrin N-terminus by EPR and fluorescence polarization.

3. Genetic analysis of the requirements for alpha-actinin function.

4. The "sticky chain": a kinetic model for the deformation of biological macromolecules.

Review 5. 3D domain swapping: as domains continue to swap.

6. Automated protein crystal structure determination using ELVES.

7. Structural organization of the nine spectrin repeats of Kalirin.

8. Separating the effects of internal friction and transition state energy to explain the slow, frustrated folding of spectrin domains.

Review 9. The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life.

10. Structural and dynamic study of the tetramerization region of non-erythroid alpha-spectrin: a frayed helix revealed by site-directed spin labeling electron paramagnetic resonance.