1ksr
From Proteopedia
(New page: 200px<br /><applet load="1ksr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ksr" /> '''THE REPEATING SEGMENTS OF THE F-ACTIN CROSS-...) |
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| - | [[Image:1ksr.gif|left|200px]]<br /><applet load="1ksr" size=" | + | [[Image:1ksr.gif|left|200px]]<br /><applet load="1ksr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ksr" /> | caption="1ksr" /> | ||
'''THE REPEATING SEGMENTS OF THE F-ACTIN CROSS-LINKING GELATION FACTOR (ABP-120) HAVE AN IMMUNOGLOBULIN FOLD, NMR, 20 STRUCTURES'''<br /> | '''THE REPEATING SEGMENTS OF THE F-ACTIN CROSS-LINKING GELATION FACTOR (ABP-120) HAVE AN IMMUNOGLOBULIN FOLD, NMR, 20 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 120,000 M(r) gelation factor and alpha-actinin are among the most | + | 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== | ==About this Structure== | ||
| - | 1KSR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http:// | + | 1KSR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KSR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Fucini, P.]] | [[Category: Fucini, P.]] | ||
[[Category: Herberhold, C.]] | [[Category: Herberhold, C.]] | ||
| - | [[Category: Holak, T | + | [[Category: Holak, T A.]] |
| - | [[Category: Noegel, A | + | [[Category: Noegel, A A.]] |
[[Category: Renner, C.]] | [[Category: Renner, C.]] | ||
[[Category: abp-120]] | [[Category: abp-120]] | ||
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[[Category: structure]] | [[Category: structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:32 2008'' |
Revision as of 11:37, 21 February 2008
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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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