1CUN
CRYSTAL STRUCTURE OF REPEATS 16 AND 17 OF CHICKEN BRAIN ALPHA SPECTRIN
Summary for 1CUN
| Entry DOI | 10.2210/pdb1cun/pdb |
| Descriptor | PROTEIN (ALPHA SPECTRIN) (2 entities in total) |
| Functional Keywords | two repeats of spectrin, alpha helical linker region, 2 tandem 3-helix coiled- coils, structural protein |
| Biological source | Gallus gallus (chicken) |
| Total number of polymer chains | 3 |
| Total formula weight | 73150.12 |
| Authors | Grum, V.L.,Li, D.,MacDonald, R.I.,Mondragon, A. (deposition date: 1999-08-20, release date: 1999-10-06, Last modification date: 2024-02-07) |
| Primary citation | Grum, V.L.,Li, D.,MacDonald, R.I.,Mondragon, A. Structures of two repeats of spectrin suggest models of flexibility. Cell(Cambridge,Mass.), 98:523-535, 1999 Cited by PubMed Abstract: Spectrin is a vital component of the cytoskeleton, conferring flexibility on cells and providing a scaffold for a variety of proteins. It is composed of tandem, antiparallel coiled-coil repeats. We report four related crystal structures at 1.45 A, 2.0 A, 3.1 A, and 4.0 A resolution of two connected repeats of chicken brain alpha-spectrin. In all of the structures, the linker region between adjacent units is alpha-helical without breaks, kinks, or obvious boundaries. Two features observed in the structures are (1) conformational rearrangement in one repeat, resulting in movement of the position of a loop, and (2) varying degrees of bending at the linker region. These features form the basis of two different models of flexibility: a conformational rearrangement and a bending model. These models provide novel atomic details of spectrin flexibility. PubMed: 10481916DOI: 10.1016/S0092-8674(00)81980-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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