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1quu

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1quu, resolution 2.50Å ()
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

CRYSTAL STRUCTURE OF TWO CENTRAL SPECTRIN-LIKE REPEATS FROM ALPHA-ACTININ

Publication Abstract from PubMed

We have determined the crystal structure of the two central repeats in the alpha-actinin rod at 2.5 A resolution. The repeats are connected by a helical linker and form a symmetric, antiparallel dimer in which the repeats are aligned rather than staggered. Using this structure, which reveals the structural principle that governs the architecture of alpha-actinin, we have devised a plausible model of the entire alpha-actinin rod. The electrostatic properties explain how the two alpha-actinin subunits assemble in an antiparallel fashion, placing the actin-binding sites at both ends of the rod. This molecular architecture results in a protein that is able to form cross-links between actin filaments.

Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments., Djinovic-Carugo K, Young P, Gautel M, Saraste M, Cell. 1999 Aug 20;98(4):537-46. PMID:10481917

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1quu is a 1 chain structure of Actinin with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Djinovic-Carugo K, Young P, Gautel M, Saraste M. Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments. Cell. 1999 Aug 20;98(4):537-46. PMID:10481917

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