1ksr

From Proteopedia

(Difference between revisions)

Revision as of 08:10, 23 February 2022

THE REPEATING SEGMENTS OF THE F-ACTIN CROSS-LINKING GELATION FACTOR (ABP-120) HAVE AN IMMUNOGLOBULIN FOLD, NMR, 20 STRUCTURES

Structural highlights

1ksr is a 1 chain structure with sequence from Dicdi. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	ABPC (DICDI)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GELA_DICDI] F-actin cross-linking protein.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

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

References

↑ Fucini P, Renner C, Herberhold C, Noegel AA, Holak TA. The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold. Nat Struct Biol. 1997 Mar;4(3):223-30. PMID:9164464

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ksr"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ksr' size='340' side='right'caption='[[1ksr]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ksr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1KSR FirstGlance]. <br>
+<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 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 ATCC 11735])</td></tr>
+</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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ksr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ksr OCA], [http://pdbe.org/1ksr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ksr RCSB], [http://www.ebi.ac.uk/pdbsum/1ksr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ksr ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ksr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ksr OCA], [https://pdbe.org/1ksr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ksr RCSB], [https://www.ebi.ac.uk/pdbsum/1ksr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ksr ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GELA_DICDI GELA_DICDI]] F-actin cross-linking protein.
+[[https://www.uniprot.org/uniprot/GELA_DICDI GELA_DICDI]] F-actin cross-linking protein.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 11735]]
+[[Category: Dicdi]]
 [[Category: Large Structures]]
 [[Category: Fucini, P]]

1ksr

From Proteopedia

Revision as of 08:10, 23 February 2022

THE REPEATING SEGMENTS OF THE F-ACTIN CROSS-LINKING GELATION FACTOR (ABP-120) HAVE AN IMMUNOGLOBULIN FOLD, NMR, 20 STRUCTURES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox