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PDBsum entry 3edu
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Structural protein
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PDB id
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3edu
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References listed in PDB file
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Key reference
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Title
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The structure of the ankyrin-Binding site of beta-Spectrin reveals how tandem spectrin-Repeats generate unique ligand-Binding properties.
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Authors
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P.R.Stabach,
I.Simonović,
M.A.Ranieri,
M.S.Aboodi,
T.A.Steitz,
M.Simonović,
J.S.Morrow.
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Ref.
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Blood, 2009,
113,
5377-5384.
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PubMed id
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Abstract
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Spectrin and ankyrin participate in membrane organization, stability, signal
transduction, and protein targeting; their interaction is critical for
erythrocyte stability. Repeats 14 and 15 of betaI-spectrin are crucial for
ankyrin recognition, yet the way spectrin binds ankyrin while preserving its
repeat structure is unknown. We have solved the crystal structure of the
betaI-spectrin 14,15 di-repeat unit to 2.1 A resolution and found 14 residues
critical for ankyrin binding that map to the end of the helix C of repeat 14,
the linker region, and the B-C loop of repeat 15. The tilt (64 degrees) across
the 14,15 linker is greater than in any published di-repeat structure,
suggesting that the relative positioning of the two repeats is important for
ankyrin binding. We propose that a lack of structural constraints on linker and
inter-helix loops allows proteins containing spectrin-like di-repeats to evolve
diverse but specific ligand-recognition sites without compromising the structure
of the repeat unit. The linker regions between repeats are thus critical
determinants of both spectrin's flexibility and polyfunctionality. The putative
coupling of flexibility and ligand binding suggests a mechanism by which
spectrin might participate in mechanosensory regulation.
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