1OWA

Solution Structural Studies on Human Erythrocyte Alpha Spectrin N Terminal Tetramerization Domain

Summary for 1OWA

• Entry DOI: 10.2210/pdb1owa/pdb
• Descriptor: Spectrin alpha chain, erythrocyte (1 entity in total)
• Functional Keywords: triple helical bundle, cytokine
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton: P02549
• Total number of polymer chains: 1
• Total formula weight: 18559.85

Authors

Park, S.,Caffrey, M.S.,Johnson, M.E.,Fung, L.W. (deposition date: 2003-03-28, release date: 2004-03-30, Last modification date: 2024-05-22)

Primary citation

Park, S.,Caffrey, M.S.,Johnson, M.E.,Fung, L.W.
Solution structural studies on human erythrocyte alpha-spectrin tetramerization site.
J.Biol.Chem., 278:21837-21844, 2003

PubMed Abstract: We have determined the solution NMR structure of a recombinant peptide that consists of the first 156 residues of erythroid alpha-spectrin. The first 20 residues preceding the first helix (helix C') are in a disordered conformation. The subsequent three helices (helices A1, B1, and C1) form a triple helical bundle structural domain that is similar, but not identical, to previously published structures for spectrin from Drosophila and chicken brain. Paramagnetic spin label-induced NMR resonance broadening shows that helix C', the partial domain involved in alpha- and beta-spectrin association, exhibits little interaction with the structural domain. Surprisingly, helix C' is connected to helix A1 of the structural domain by a segment of 7 residues (the junction region) that exhibits a flexible disordered conformation, in contrast to the predicted rigid helical structure. We suggest that the flexibility of this particular junction region may play an important role in modulating the association affinity of alpha- and beta-spectrin at the tetramerization site of different isoforms, such as erythroid spectrin and brain spectrin. These findings may provide insight for explaining various physiological and pathological conditions that are a consequence of varying alpha- and beta-subunit self-association affinities in their formation of the various spectrin tetramers.

PubMed: 12672815
DOI: 10.1074/jbc.M300617200

Experimental method

SOLUTION NMR