1ksr

<StructureSection load='1ksr' size='340' side='right'caption='[[1ksr]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1ksr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dicdi Dicdi]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KSR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KSR FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABPC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 DICDI])</td></tr>

[[https://www.uniprot.org/uniprot/GELA_DICDI GELA_DICDI]] F-actin cross-linking protein.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:9164464</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Dicdi]]

[[Category: Fucini, P]]

[[Category: Herberhold, C]]

[[Category: Holak, T A]]

[[Category: Noegel, A A]]

[[Category: Renner, C]]

[[Category: Immunoglobulin]]