Crystal Structure of the Nonerythroid α-Spectrin Tetramerization Site Reveals Differences between Erythroid and Nonerythroid Spectrin Tetramer Formation

We have solved the crystal structure of a segment of nonerythroid α-spectrin (αII) consisting of the first 147 residues to a resolution of 2.3 Å. We find that the structure of this segment is generally similar to a corresponding segment from erythroid α-spectrin (αI) but exhibits unique differences...

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Bibliografiske detaljer
Main Authors: Mehboob, Shahila, Song, Yuanli, Witek, Marta, Long, Fei, Santarsiero, Bernard D., Johnson, Michael E., Fung, Leslie W.-M.
Format: Artigo
Sprog:Inglês
Udgivet: American Society for Biochemistry and Molecular Biology 2010
Fag:
Protein Structure and Folding
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC2863205/
https://ncbi.nlm.nih.gov/pubmed/20228407
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.080028
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