First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.
1x67
From Proteopedia
| 1x67, 20 NMR models () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Gene: | DBNL (Homo sapiens) | ||||||||
| |||||||||
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB, TOPSAN | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Solution structure of the cofilin homology domain of HIP-55 (drebrin-like protein)
Actin is one of the most conserved proteins in nature. Its assembly and disassembly are regulated by many proteins, including the family of actin-depolymerizing factor homology (ADF-H) domains. ADF-H domains can be divided into five classes: ADF/cofilin, glia maturation factor (GMF), coactosin, twinfilin, and Abp1/drebrin. The best-characterized class is ADF/cofilin. The other four classes have drawn much less attention and very few structures have been reported. This study presents the solution NMR structure of the ADF-H domain of human HIP-55-drebrin-like protein, the first published structure of a drebrin-like domain (mammalian), and the first published structure of GMF beta (mouse). We also determined the structures of mouse GMF gamma, the mouse coactosin-like domain and the C-terminal ADF-H domain of mouse twinfilin 1. Although the overall fold of the five domains is similar, some significant differences provide valuable insights into filamentous actin (F-actin) and globular actin (G-actin) binding, including the identification of binding residues on the long central helix. This long helix is stabilized by three or four residues. Notably, the F-actin binding sites of mouse GMF beta and GMF gamma contain two additional beta-strands not seen in other ADF-H structures. The G-actin binding site of the ADF-H domain of human HIP-55-drebrin-like protein is absent and distorted in mouse GMF beta and GMF gamma.
NMR solution structures of actin depolymerizing factor homology domains., Goroncy AK, Koshiba S, Tochio N, Tomizawa T, Sato M, Inoue M, Watanabe S, Hayashizaki Y, Tanaka A, Kigawa T, Yokoyama S, Protein Sci. 2009 Nov;18(11):2384-92. PMID:19768801
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1X67 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA.
Reference
- Goroncy AK, Koshiba S, Tochio N, Tomizawa T, Sato M, Inoue M, Watanabe S, Hayashizaki Y, Tanaka A, Kigawa T, Yokoyama S. NMR solution structures of actin depolymerizing factor homology domains. Protein Sci. 2009 Nov;18(11):2384-92. PMID:19768801 doi:10.1002/pro.248
Page seeded by OCA on Wed Feb 3 08:58:42 2010
Categories: Homo sapiens | Goroncy, A K. | Inoue, M. | Kigawa, T. | Kobayashi, N. | Koshiba, S. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Sato, M. | Tochio, N. | Yokoyama, S. | Actin-binding protein | C-jun n-terminal kinase activation | Cell-free protein synthesis | Hpk-1 activation | Mabp1 | National project on protein structural and functional analyse | Nppsfa | Protein binding | Riken structural genomics/proteomics initiative | Rsgi | Sh3p7 | Structural genomic | T-cell antigen receptor regulation | T-cell lymphocyte signaling and regulation
