Conformational change of erythroid alpha-spectrin at the tetramerization site upon binding beta-spectrin.

Conformational change of erythroid alpha-spectrin at the tetramerization site upon binding beta-spectrin. Research Abstract Details 

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Conformational change of erythroid alpha-spectrin at the tetramerization site upon binding beta-spectrin. Abstract Text:

Fei Long,Dan McElheny,Shaokai Jiang,Sunghyouk Park,Michael S Caffrey,Leslie W-M Fung,Fei Long,Dan McElheny,Shaokai Jiang,Sunghyouk Park,Michael S Caffrey,Leslie W-M Fung,

We previously determined the solution structures of the first 156 residues of human erythroid alpha-spectrin (SpalphaI-1-156, or simply Spalpha). Spalpha consists of the tetramerization site of alpha-spectrin and associates with a model beta-spectrin protein (Spbeta) with an affinity similar to that of native alpha- and beta-spectrin. Upon alphabeta-complex formation, our previous results indicate that there is an increase in helicity in the complex, suggesting conformational change in either Spalpha or Spbeta or in both. We have now used isothermal titration calorimetry, circular dichroism, static and dynamic light scattering, and solution NMR methods to investigate properties of the complex as well as the conformation of Spalpha in the complex. The results reveal a highly asymmetric complex, with a Perrin shape parameter of 1.23, which could correspond to a prolate ellipsoid with a major axis of about five and a minor axis of about one. We identified 12 residues, five prior to and seven following the partial domain helix in Spalpha that moved freely relative to the structural domain in the absence of Spbeta but when in the complex moved with a mobility similar to that of the structural domain. Thus, it appears that the association with Spbeta induced an unstructured-to-helical conformational transition in these residues to produce a rigid and asymmetric complex. Our findings may provide insight toward understanding different association affinities of alphabeta-spectrin at the tetramerization site for erythroid and non-erythroid spectrin and a possible mechanism to understand some of the clinical mutations, such as L49F of alpha-spectrin, which occur outside the functional partial domain region.

Conformational change of erythroid alpha-spectrin at the tetramerization site upon binding beta-spectrin. Publishing Authors By Initials

F Long,D McElheny,S Jiang,S Park,MS Caffrey,LW Fung,F Long,D McElheny,S Jiang,S Park,MS Caffrey,LW Fung,

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Conformational change of erythroid alpha-spectrin at the tetramerization site upon binding beta-spectrin. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Protein science : a publication of the Protein Soc

VOLUME: 16

Page Numbers: 2519-30

Journal Abbreviation: Protein Sci.

ISSN: 0961-8368

DAY: 28

MONTH: 09

YEAR: 2007

Conformational change of erythroid alpha-spectrin at the tetramerization site upon binding beta-spectrin. Information

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LANGUAGE: eng

NlmUniqueID: 9211750

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Grant and Affiliation Information for Conformational change of erythroid alpha-spectrin at the tetramerization site upon binding beta-spectrin.

AFFILIATION: Department of Chemistry, University of Illinois at Chicago 60607, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: P41 GM68944

ACRONYM: GM

MEDLINETA: Protein Sci

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