2SPC
CRYSTAL STRUCTURE OF THE REPETITIVE SEGMENTS OF SPECTRIN
Summary for 2SPC
Entry DOI | 10.2210/pdb2spc/pdb |
Descriptor | SPECTRIN (2 entities in total) |
Functional Keywords | cytoskeleton |
Biological source | Drosophila melanogaster (fruit fly) |
Total number of polymer chains | 2 |
Total formula weight | 24585.46 |
Authors | Yan, Y.,Winograd, E.,Viel, A.,Cronin, T.,Harrison, S.C.,Branton, D. (deposition date: 1994-03-01, release date: 1994-05-31, Last modification date: 2024-02-21) |
Primary citation | Yan, Y.,Winograd, E.,Viel, A.,Cronin, T.,Harrison, S.C.,Branton, D. Crystal structure of the repetitive segments of spectrin. Science, 262:2027-2030, 1993 Cited by PubMed 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. PubMed: 8266097PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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