| Structural highlights
4b1x is a 2 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , |
| Related: | 1alm, 1atn, 1eqy, 1esv, 1h1v, 1ijj, 1j6z, 1kxp, 1lcu, 1lot, 1m8q, 1ma9, 1mvw, 1nwk, 1o18, 1o19, 1o1a, 1o1b, 1o1c, 1o1d, 1o1e, 1o1f, 1o1g, 1p8z, 1qz5, 1qz6, 1rdw, 1rfq, 1rgi, 1s22, 1sqk, 1t44, 1uy5, 1wua, 1y64, 2a3z, 2a40, 2a41, 2a42, 2a5x, 2asm, 2aso, 2asp, 2d1k, 2ff3, 2ff6, 2fxu, 2v51, 2v52, 2vcp, 2vyp, 2w49, 2w4u, 2y83, 2yje, 2yjf, 4a7h, 4a7l, 4a7n, 4b1u, 4b1v, 4b1w, 4b1y, 4b1z |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [PHAR1_MOUSE] Binds actin monomers (G actin) and plays a role in the reorganization of the actin cytoskeleton and in formation of actin stress fibers. Plays a role in the formation of tubules by endothelial cells. Regulates PPP1CA activity. Required for normal cell survival (By similarity). Plays a role in cell motility.[1] [2]
Publication Abstract from PubMed
The Phactr family of PP1-binding proteins and the myocardin-related transcription factor family of transcriptional coactivators contain regulatory domains comprising three copies of the RPEL motif, a G-actin binding element. We report the structure of a Phactr1 G-actinRPEL domain complex. Three G-actins surround the crank-shaped RPEL domain forming a closed helical assembly. Their spatial relationship is identical to the RPEL-actins within the pentavalent MRTF G-actinRPEL domain complex, suggesting that conserved cooperative interactions between actinRPEL units organize the assembly. In the trivalent Phactr1 complex, each G-actinRPEL unit makes secondary contacts with its downstream actin involving distinct RPEL residues. Similar secondary contacts are seen in G-actinRPEL peptide crystals. Loss-of-secondary-contact mutations destabilize the Phactr1 G-actinRPEL assembly. Furthermore, actin-mediated inhibition of Phactr1 nuclear import requires secondary contact residues in the Phactr1 N-terminal RPEL-N motif, suggesting that it involves interaction of RPEL-N with the C-terminal assembly. Secondary actin contacts by actin-bound RPEL motifs thus govern formation of multivalent actinRPEL assemblies.
Structures of the Phactr1 RPEL Domain and RPEL Motif Complexes with G-Actin Reveal the Molecular Basis for Actin Binding Cooperativity.,Mouilleron S, Wiezlak M, O'Reilly N, Treisman R, McDonald NQ Structure. 2012 Oct 2. pii: S0969-2126(12)00335-8. doi:, 10.1016/j.str.2012.08.031. PMID:23041370[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wiezlak M, Diring J, Abella J, Mouilleron S, Way M, McDonald NQ, Treisman R. G-actin regulates the shuttling and PP1 binding of the RPEL protein Phactr1 to control actomyosin assembly. J Cell Sci. 2012 Dec 1;125(Pt 23):5860-72. doi: 10.1242/jcs.112078. Epub 2012 Sep, 12. PMID:22976292 doi:10.1242/jcs.112078
- ↑ Mouilleron S, Wiezlak M, O'Reilly N, Treisman R, McDonald NQ. Structures of the Phactr1 RPEL Domain and RPEL Motif Complexes with G-Actin Reveal the Molecular Basis for Actin Binding Cooperativity. Structure. 2012 Oct 2. pii: S0969-2126(12)00335-8. doi:, 10.1016/j.str.2012.08.031. PMID:23041370 doi:10.1016/j.str.2012.08.031
- ↑ Mouilleron S, Wiezlak M, O'Reilly N, Treisman R, McDonald NQ. Structures of the Phactr1 RPEL Domain and RPEL Motif Complexes with G-Actin Reveal the Molecular Basis for Actin Binding Cooperativity. Structure. 2012 Oct 2. pii: S0969-2126(12)00335-8. doi:, 10.1016/j.str.2012.08.031. PMID:23041370 doi:10.1016/j.str.2012.08.031
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