1S35

Crystal Structure of Repeats 8 and 9 of Human Erythroid Spectrin

Summary for 1S35

• Entry DOI: 10.2210/pdb1s35/pdb
• Descriptor: Spectrin beta chain, erythrocyte, SULFATE ION (3 entities in total)
• Functional Keywords: two repeats of spectrin, alpha helical linker region, 3-helix coiled-coils, beta spectrin, structural protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton: P11277
• Total number of polymer chains: 1
• Total formula weight: 24461.93

Authors

Kusunoki, H.,MacDonald, R.I.,Mondragon, A. (deposition date: 2004-01-12, release date: 2004-04-20, Last modification date: 2024-02-14)

Primary citation

Kusunoki, H.,MacDonald, R.I.,Mondragon, A.
Structural insights into the stability and flexibility of unusual erythroid spectrin repeats
Structure, 12:645-656, 2004

PubMed Abstract: Erythroid spectrin, a major component of the cytoskeletal network of the red cell which contributes to both the stability and the elasticity of the red cell membrane, is composed of two subunits, alpha and beta, each formed by 16-20 tandem repeats. The properties of the repeats and their relative arrangement are thought to be key determinants of spectrin flexibility. Here we report a 2.4 A resolution crystal structure of human erythroid beta-spectrin repeats 8 and 9. This two-repeat fragment is unusual as it exhibits low stability of folding and one of its repeats lacks two tryptophans highly conserved among spectrin repeats. Two key factors responsible for the lower stability and, possibly, its flexibility, are revealed by the structure. A third novel feature of the structure is the relative orientation of the two repeats, which increases the range of possible conformations and provides new insights into atomic models of spectrin flexibility.

PubMed: 15062087
DOI: 10.1016/j.str.2004.02.022

Experimental method

X-RAY DIFFRACTION (2.4 Å)