1ksr
From Proteopedia
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THE REPEATING SEGMENTS OF THE F-ACTIN CROSS-LINKING GELATION FACTOR (ABP-120) HAVE AN IMMUNOGLOBULIN FOLD, NMR, 20 STRUCTURES
Overview
The 120,000 M(r) gelation factor and alpha-actinin are among the most, abundant F-actin cross-linking proteins in Dictyostelium discoideum. Both, molecules are rod-shaped homodimers. Each monomer chain is comprised of an, actin-binding domain and a rod domain. The rod domain of the gelation, factor consists of six 100-residue repetitive segments with high internal, homology. We have now determined the three-dimensional structure of, segment 4 of the rod domain of the gelation factor from D. discoideum, using NMR spectroscopy. The segment consists of seven beta-sheets arranged, in an immunoglobulin-like (Ig) fold. This is completely different from the, alpha-actinin rod domain which consists of four spectrin-like, alpha-helical segments. The gelation factor is the first example of an, Ig-fold found in an actin-binding protein. Two highly homologous, actin-binding proteins from human with similar sequences to the gelation, factor, filamin and a 280,000 M(r) actin-binding protein (ABP-280), share, conserved residues that form the core of the gelation factor repetitive, segment structure. Thus, the segment 4 structure should be common to this, subfamily of the spectrin superfamily. The structure of segment 4 together, with previously published electron microscopy data, provide an explanation, for the dimerization of the whole gelation factor molecule.
About this Structure
1KSR is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.
Reference
The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold., Fucini P, Renner C, Herberhold C, Noegel AA, Holak TA, Nat Struct Biol. 1997 Mar;4(3):223-30. PMID:9164464
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