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PDBsum entry 1ux5

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Structural protein PDB id
1ux5

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
411 a.a. *
Waters ×31
* Residue conservation analysis
PDB id:
1ux5
Name: Structural protein
Title: Crystal structures of a formin homology-2 domain reveal a flexibly tethered dimer architecture
Structure: Bni1 protein. Chain: a. Fragment: fh2 domain, residues 1350-1760. Synonym: formin, synthetic lethal 39. Engineered: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PDB file)
Resolution:
2.50Å     R-factor:   0.207     R-free:   0.251
Authors: Y.Xu,J.B.Moseley,I.Sagot,F.Poy,D.Pellman,B.L.Goode,M.J.Eck
Key ref:
Y.Xu et al. (2004). Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture. Cell, 116, 711-723. PubMed id: 15006353 DOI: 10.1016/S0092-8674(04)00210-7
Date:
19-Feb-04     Release date:   11-Mar-04    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P41832  (BNI1_YEAST) -  Protein BNI1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1953 a.a.
411 a.a.
Key:    PfamA domain  Secondary structure

 

 
DOI no: 10.1016/S0092-8674(04)00210-7 Cell 116:711-723 (2004)
PubMed id: 15006353  
 
 
Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture.
Y.Xu, J.B.Moseley, I.Sagot, F.Poy, D.Pellman, B.L.Goode, M.J.Eck.
 
  ABSTRACT  
 
Formin proteins participate in a wide range of cytoskeletal processes in all eukaryotes. The defining feature of formins is a highly conserved approximately 400 residue region, the Formin Homology-2 (FH2) domain, which has recently been found to nucleate actin filaments. Here we report crystal structures of the S. cerevesiae Bni1p FH2 domain. The mostly alpha-helical FH2 domain forms a unique "tethered dimer" in which two elongated actin binding heads are tied together at either end by an unusual lasso and linker structure. Biochemical and crystallographic observations indicate that the dimer is stable but flexible, with flexibility between the two halves of the dimer conferred by the linker segments. Although each half of the dimer is competent to interact with filament ends, the intact dimer is required for actin nucleation and processive capping. The tethered dimer architecture may allow formins to stair-step on the barbed end of an elongating nascent filament.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Three-Dimensional Structure of the FH2 Domain Dimmer
Figure 7.
Figure 7. A Speculative Model Showing How the Tethered Dimer Architecture of the FH2 Domain Could Allow Stair-Stepping on the Elongating Barbed End of F-Actin
 
  The above figures are reprinted by permission from Cell Press: Cell (2004, 116, 711-723) copyright 2004.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
23222643 M.E.Thompson, E.G.Heimsath, T.J.Gauvin, H.N.Higgs, and F.J.Kull (2013).
FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation.
  Nat Struct Mol Biol, 20, 111-118.
PDB code: 4eah
21873984 B.Yu, H.C.Cheng, C.A.Brautigam, D.R.Tomchick, and M.K.Rosen (2011).
Mechanism of actin filament nucleation by the bacterial effector VopL.
  Nat Struct Mol Biol, 18, 1068-1074.
PDB code: 3seo
21481778 E.Karaca, and A.M.Bonvin (2011).
A multidomain flexible docking approach to deal with large conformational changes in the modeling of biomolecular complexes.
  Structure, 19, 555-565.  
21282620 P.O.Widlund, J.H.Stear, A.Pozniakovsky, M.Zanic, S.Reber, G.J.Brouhard, A.A.Hyman, and J.Howard (2011).
XMAP215 polymerase activity is built by combining multiple tubulin-binding TOG domains and a basic lattice-binding region.
  Proc Natl Acad Sci U S A, 108, 2741-2746.  
21314430 R.Dominguez, and K.C.Holmes (2011).
Actin structure and function.
  Annu Rev Biophys, 40, 169-186.  
21307369 X.H.Xue, C.Q.Guo, F.Du, Q.L.Lu, C.M.Zhang, and H.Y.Ren (2011).
AtFH8 is involved in root development under effect of low-dose latrunculin B in dividing cells.
  Mol Plant, 4, 264-278.  
20538977 A.M.Ducka, P.Joel, G.M.Popowicz, K.M.Trybus, M.Schleicher, A.A.Noegel, R.Huber, T.A.Holak, and T.Sitar (2010).
Structures of actin-bound Wiskott-Aldrich syndrome protein homology 2 (WH2) domains of Spire and the implication for filament nucleation.
  Proc Natl Acad Sci U S A, 107, 11757-11762.
PDB codes: 3mmv 3mn5 3mn6 3mn7 3mn9
  20927338 A.Nezami, F.Poy, A.Toms, W.Zheng, and M.J.Eck (2010).
Crystal structure of a complex between amino and carboxy terminal fragments of mDia1: insights into autoinhibition of diaphanous-related formins.
  PLoS One, 5, 0.
PDB code: 3o4x
20226666 A.Yonetani, and F.Chang (2010).
Regulation of cytokinesis by the formin cdc12p.
  Curr Biol, 20, 561-566.  
  20862687 E.S.Harris, T.J.Gauvin, E.G.Heimsath, and H.N.Higgs (2010).
Assembly of filopodia by the formin FRL2 (FMNL3).
  Cytoskeleton (Hoboken), 67, 755-772.  
20536448 H.G.Mannherz, A.J.Mazur, and B.Jockusch (2010).
Repolymerization of actin from actin:thymosin beta4 complex induced by diaphanous related formins and gelsolin.
  Ann N Y Acad Sci, 1194, 36-43.  
20071330 H.I.Balcer, K.Daugherty-Clarke, and B.L.Goode (2010).
The p40/ARPC1 subunit of Arp2/3 complex performs multiple essential roles in WASp-regulated actin nucleation.
  J Biol Chem, 285, 8481-8491.  
20237478 K.G.Campellone, and M.D.Welch (2010).
A nucleator arms race: cellular control of actin assembly.
  Nat Rev Mol Cell Biol, 11, 237-251.  
20881207 L.Andrés-Delgado, O.M.Antón, R.Madrid, J.A.Byrne, and M.A.Alonso (2010).
Formin INF2 regulates MAL-mediated transport of Lck to the plasma membrane of human T lymphocytes.
  Blood, 116, 5919-5929.  
19997130 M.A.Chesarone, A.G.DuPage, and B.L.Goode (2010).
Unleashing formins to remodel the actin and microtubule cytoskeletons.
  Nat Rev Mol Cell Biol, 11, 62-74.  
20177055 S.Barkó, B.Bugyi, M.F.Carlier, R.Gombos, T.Matusek, J.Mihály, and M.Nyitrai (2010).
Characterization of the biochemical properties and biological function of the formin homology domains of Drosophila DAAM.
  J Biol Chem, 285, 13154-13169.  
20446344 S.H.Lee, and R.Dominguez (2010).
Regulation of actin cytoskeleton dynamics in cells.
  Mol Cells, 29, 311-325.  
21149568 T.Iskratsch, S.Lange, J.Dwyer, A.L.Kho, C.dos Remedios, and E.Ehler (2010).
Formin follows function: a muscle-specific isoform of FHOD3 is regulated by CK2 phosphorylation and promotes myofibril maintenance.
  J Cell Biol, 191, 1159-1172.  
  20927343 T.Otomo, D.R.Tomchick, C.Otomo, M.Machius, and M.K.Rosen (2010).
Crystal structure of the Formin mDia1 in autoinhibited conformation.
  PLoS One, 5, 0.
PDB code: 3obv
20949068 W.Daher, F.Plattner, M.F.Carlier, and D.Soldati-Favre (2010).
Concerted action of two formins in gliding motility and host cell invasion by Toxoplasma gondii.
  PLoS Pathog, 6, 0.  
19251693 A.S.Paul, and T.D.Pollard (2009).
Energetic Requirements for Processive Elongation of Actin Filaments by FH1FH2-formins.
  J Biol Chem, 284, 12533-12540.  
19459187 A.S.Paul, and T.D.Pollard (2009).
Review of the mechanism of processive actin filament elongation by formins.
  Cell Motil Cytoskeleton, 66, 606-617.  
19470758 D.Kumar, and A.B.Lassar (2009).
The transcriptional activity of Sox9 in chondrocytes is regulated by RhoA signaling and actin polymerization.
  Mol Cell Biol, 29, 4262-4273.  
19386598 K.K.Wen, and P.A.Rubenstein (2009).
Differential regulation of actin polymerization and structure by yeast formin isoforms.
  J Biol Chem, 284, 16776-16783.  
19706596 K.Taniguchi, R.Takeya, S.Suetsugu, M.Kan-O, M.Narusawa, A.Shiose, R.Tominaga, and H.Sumimoto (2009).
Mammalian formin fhod3 regulates actin assembly and sarcomere organization in striated muscles.
  J Biol Chem, 284, 29873-29881.  
19764708 T.J.Gauvin, J.Fukui, J.R.Peterson, and H.N.Higgs (2009).
Isoform-selective chemical inhibition of mDia-mediated actin assembly.
  Biochemistry, 48, 9327-9329.  
18160294 A.S.Paul, A.Paul, T.D.Pollard, and T.Pollard (2008).
The role of the FH1 domain and profilin in formin-mediated actin-filament elongation and nucleation.
  Curr Biol, 18, 9.  
18786395 A.Schulte, B.Stolp, A.Schönichen, O.Pylypenko, A.Rak, O.T.Fackler, and M.Geyer (2008).
The human formin FHOD1 contains a bipartite structure of FH3 and GTPase-binding domains required for activation.
  Structure, 16, 1313-1323.
PDB code: 3dad
18305104 A.Yonetani, R.J.Lustig, J.B.Moseley, T.Takeda, B.L.Goode, and F.Chang (2008).
Regulation and targeting of the fission yeast formin cdc12p in cytokinesis.
  Mol Biol Cell, 19, 2208-2219.  
18786389 C.Baarlink, and R.Grosse (2008).
A GBD uncovered: the FHOD1 N terminus is formin'.
  Structure, 16, 1287-1288.  
18840602 D.Chalkia, N.Nikolaidis, W.Makalowski, J.Klein, and M.Nei (2008).
Origins and evolution of the formin multigene family that is involved in the formation of actin filaments.
  Mol Biol Evol, 25, 2717-2733.  
18577519 E.M.Neidt, C.T.Skau, and D.R.Kovar (2008).
The cytokinesis formins from the nematode worm and fission yeast differentially mediate actin filament assembly.
  J Biol Chem, 283, 23872-23883.  
18458159 F.Bartolini, J.B.Moseley, J.Schmoranzer, L.Cassimeris, B.L.Goode, and G.G.Gundersen (2008).
The formin mDia2 stabilizes microtubules independently of its actin nucleation activity.
  J Cell Biol, 181, 523-536.  
19116660 H.Wang, and D.Vavylonis (2008).
Model of For3p-mediated actin cable assembly in fission yeast.
  PLoS ONE, 3, e4078.  
  18329618 J.Baum, C.J.Tonkin, A.S.Paul, M.Rug, B.J.Smith, S.B.Gould, D.Richard, T.D.Pollard, and A.F.Cowman (2008).
A malaria parasite formin regulates actin polymerization and localizes to the parasite-erythrocyte moving junction during invasion.
  Cell Host Microbe, 3, 188-198.  
18560567 M.Dettenhofer, F.Zhou, and P.Leder (2008).
Formin 1-isoform IV deficient cells exhibit defects in cell spreading and focal adhesion formation.
  PLoS ONE, 3, e2497.  
18829452 M.Lammers, S.Meyer, D.Kühlmann, and A.Wittinghofer (2008).
Specificity of Interactions between mDia Isoforms and Rho Proteins.
  J Biol Chem, 283, 35236-35246.
PDB code: 3eg5
18707582 N.A.Gloushankova (2008).
Changes in regulation of cell-cell adhesion during tumor transformation.
  Biochemistry (Mosc), 73, 742-750.  
18287523 S.Watanabe, Y.Ando, S.Yasuda, H.Hosoya, N.Watanabe, T.Ishizaki, and S.Narumiya (2008).
mDia2 induces the actin scaffold for the contractile ring and stabilizes its position during cytokinesis in NIH 3T3 cells.
  Mol Biol Cell, 19, 2328-2338.  
18218625 T.Higashi, T.Ikeda, R.Shirakawa, H.Kondo, M.Kawato, M.Horiguchi, T.Okuda, K.Okawa, S.Fukai, O.Nureki, T.Kita, and H.Horiuchi (2008).
Biochemical characterization of the Rho GTPase-regulated actin assembly by diaphanous-related formins, mDia1 and Daam1, in platelets.
  J Biol Chem, 283, 8746-8755.  
18162551 W.Liu, A.Sato, D.Khadka, R.Bharti, H.Diaz, L.W.Runnels, and R.Habas (2008).
Mechanism of activation of the Formin protein Daam1.
  Proc Natl Acad Sci U S A, 105, 210-215.  
17373907 B.L.Goode, and M.J.Eck (2007).
Mechanism and function of formins in the control of actin assembly.
  Annu Rev Biochem, 76, 593-627.  
17569543 B.Wawro, N.J.Greenfield, M.A.Wear, J.A.Cooper, H.N.Higgs, and S.E.Hitchcock-DeGregori (2007).
Tropomyosin regulates elongation by formin at the fast-growing end of the actin filament.
  Biochemistry, 46, 8146-8155.  
17620407 D.T.Brandt, S.Marion, G.Griffiths, T.Watanabe, K.Kaibuchi, and R.Grosse (2007).
Dia1 and IQGAP1 interact in cell migration and phagocytic cup formation.
  J Cell Biol, 178, 193-200.  
17347519 H.O.Park, and E.Bi (2007).
Central roles of small GTPases in the development of cell polarity in yeast and beyond.
  Microbiol Mol Biol Rev, 71, 48-96.  
17482208 J.Lu, W.Meng, F.Poy, S.Maiti, B.L.Goode, and M.J.Eck (2007).
Structure of the FH2 domain of Daam1: implications for formin regulation of actin assembly.
  J Mol Biol, 369, 1258-1269.
PDB code: 2j1d
17923532 M.E.Quinlan, S.Hilgert, A.Bedrossian, R.D.Mullins, and E.Kerkhoff (2007).
Regulatory interactions between two actin nucleators, Spire and Cappuccino.
  J Cell Biol, 179, 117-128.  
17986009 M.Yamashita, T.Higashi, S.Suetsugu, Y.Sato, T.Ikeda, R.Shirakawa, T.Kita, T.Takenawa, H.Horiuchi, S.Fukai, and O.Nureki (2007).
Crystal structure of human DAAM1 formin homology 2 domain.
  Genes Cells, 12, 1255-1265.
PDB code: 2z6e
17699595 S.G.Martin, S.A.Rincón, R.Basu, P.Pérez, and F.Chang (2007).
Regulation of the formin for3p by cdc42p and bud6p.
  Mol Biol Cell, 18, 4155-4167.  
17344480 S.M.Buttery, S.Yoshida, and D.Pellman (2007).
Yeast formins Bni1 and Bnr1 utilize different modes of cortical interaction during the assembly of actin cables.
  Mol Biol Cell, 18, 1826-1838.  
17477841 T.D.Pollard (2007).
Regulation of actin filament assembly by Arp2/3 complex and formins.
  Annu Rev Biophys Biomol Struct, 36, 451-477.  
17575049 T.M.Kitzing, A.S.Sahadevan, D.T.Brandt, H.Knieling, S.Hannemann, O.T.Fackler, J.Grosshans, and R.Grosse (2007).
Positive feedback between Dia1, LARG, and RhoA regulates cell morphology and invasion.
  Genes Dev, 21, 1478-1483.  
16361249 A.Schönichen, M.Alexander, J.E.Gasteier, F.E.Cuesta, O.T.Fackler, and M.Geyer (2006).
Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1.
  J Biol Chem, 281, 5084-5093.  
16943183 A.Seth, C.Otomo, and M.K.Rosen (2006).
Autoinhibition regulates cellular localization and actin assembly activity of the diaphanous-related formins FRLalpha and mDia1.
  J Cell Biol, 174, 701-713.  
16490788 B.Bugyi, G.Papp, G.Hild, D.Lõrinczy, E.M.Nevalainen, P.Lappalainen, B.Somogyi, and M.Nyitrai (2006).
Formins regulate actin filament flexibility through long range allosteric interactions.
  J Biol Chem, 281, 10727-10736.  
16361707 B.J.Wallar, B.N.Stropich, J.A.Schoenherr, H.A.Holman, S.M.Kitchen, and A.S.Alberts (2006).
The basic region of the diaphanous-autoregulatory domain (DAD) is required for autoregulatory interactions with the diaphanous-related formin inhibitory domain.
  J Biol Chem, 281, 4300-4307.  
16364624 D.R.Kovar (2006).
Molecular details of formin-mediated actin assembly.
  Curr Opin Cell Biol, 18, 11-17.  
16439214 D.R.Kovar, E.S.Harris, R.Mahaffy, H.N.Higgs, and T.D.Pollard (2006).
Control of the assembly of ATP- and ADP-actin by formins and profilin.
  Cell, 124, 423-435.  
16483928 D.Vavylonis, D.R.Kovar, B.O'Shaughnessy, and T.D.Pollard (2006).
Model of formin-associated actin filament elongation.
  Mol Cell, 21, 455-466.  
16556604 E.S.Harris, I.Rouiller, D.Hanein, and H.N.Higgs (2006).
Mechanistic differences in actin bundling activity of two mammalian formins, FRL1 and mDia2.
  J Biol Chem, 281, 14383-14392.  
16829561 G.Papp, B.Bugyi, Z.Ujfalusi, S.Barkó, G.Hild, B.Somogyi, and M.Nyitrai (2006).
Conformational changes in actin filaments induced by formin binding to the barbed end.
  Biophys J, 91, 2564-2572.  
16236798 H.P.Schmitz, A.Kaufmann, M.Köhli, P.P.Laissue, and P.Philippsen (2006).
From function to shape: a novel role of a formin in morphogenesis of the fungus Ashbya gossypii.
  Mol Biol Cell, 17, 130-145.  
16959963 J.B.Moseley, and B.L.Goode (2006).
The yeast actin cytoskeleton: from cellular function to biochemical mechanism.
  Microbiol Mol Biol Rev, 70, 605-645.  
16651381 P.Hotulainen, and P.Lappalainen (2006).
Stress fibers are generated by two distinct actin assembly mechanisms in motile cells.
  J Cell Biol, 173, 383-394.  
16782006 S.G.Martin, and F.Chang (2006).
Dynamics of the formin for3p in actin cable assembly.
  Curr Biol, 16, 1161-1170.  
16243528 A.Piekny, M.Werner, and M.Glotzer (2005).
Cytokinesis: welcome to the Rho zone.
  Trends Cell Biol, 15, 651-658.  
15908944 A.Schirenbeck, T.Bretschneider, R.Arasada, M.Schleicher, and J.Faix (2005).
The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia.
  Nat Cell Biol, 7, 619-625.  
15854898 B.Baum, and P.Kunda (2005).
Actin nucleation: spire - actin nucleator in a class of its own.
  Curr Biol, 15, R305-R308.  
15591319 F.Li, and H.N.Higgs (2005).
Dissecting requirements for auto-inhibition of actin nucleation by the formin, mDia1.
  J Biol Chem, 280, 6986-6992.  
15740615 F.Rivero, T.Muramoto, A.K.Meyer, H.Urushihara, T.Q.Uyeda, and C.Kitayama (2005).
A comparative sequence analysis reveals a common GBD/FH3-FH1-FH2-DAD architecture in formins from Dictyostelium, fungi and metazoa.
  BMC Genomics, 6, 28.  
15509653 H.N.Higgs, K.J.Peterson, and K.J.Peterson (2005).
Phylogenetic analysis of the formin homology 2 domain.
  Mol Biol Cell, 16, 1.  
15950879 H.N.Higgs (2005).
Formin proteins: a domain-based approach.
  Trends Biochem Sci, 30, 342-353.  
15923184 J.B.Moseley, and B.L.Goode (2005).
Differential activities and regulation of Saccharomyces cerevisiae formin proteins Bni1 and Bnr1 by Bud6.
  J Biol Chem, 280, 28023-28033.  
16183906 J.L.D'Agostino, and B.L.Goode (2005).
Dissection of Arp2/3 complex actin nucleation mechanism and distinct roles for its nucleation-promoting factors in Saccharomyces cerevisiae.
  Genetics, 171, 35-47.  
15765105 M.Ingouff, J.N.Fitz Gerald, C.Guérin, H.Robert, M.B.Sørensen, D.Van Damme, D.Geelen, L.Blanchoin, and F.Berger (2005).
Plant formin AtFH5 is an evolutionarily conserved actin nucleator involved in cytokinesis.
  Nat Cell Biol, 7, 374-380.  
16313636 M.J.Deeks, F.Cvrcková, L.M.Machesky, V.Mikitová, T.Ketelaar, V.Zársky, B.Davies, and P.J.Hussey (2005).
Arabidopsis group Ie formins localize to specific cell membrane domains, interact with actin-binding proteins and cause defects in cell expansion upon aberrant expression.
  New Phytol, 168, 529-540.  
16292343 M.Lammers, R.Rose, A.Scrima, and A.Wittinghofer (2005).
The regulation of mDia1 by autoinhibition and its release by Rho*GTP.
  EMBO J, 24, 4176-4187.
PDB code: 2bap
  16511001 R.Rose, A.Wittinghofer, and M.Weyand (2005).
The purification and crystallization of mDia1 in complex with RhoC.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 225-227.  
15864301 R.Rose, M.Weyand, M.Lammers, T.Ishizaki, M.R.Ahmadian, and A.Wittinghofer (2005).
Structural and mechanistic insights into the interaction between Rho and mammalian Dia.
  Nature, 435, 513-518.
PDB codes: 1z2c 1z2h
16166638 S.E.Tcheperegine, X.D.Gao, and E.Bi (2005).
Regulation of cell polarity by interactions of Msb3 and Msb4 with Cdc42 and polarisome components.
  Mol Cell Biol, 25, 8567-8580.  
15635372 T.Otomo, D.R.Tomchick, C.Otomo, S.C.Panchal, M.Machius, and M.K.Rosen (2005).
Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain.
  Nature, 433, 488-494.
PDB code: 1y64
16157699 T.Shemesh, T.Otomo, M.K.Rosen, A.D.Bershadsky, and M.M.Kozlov (2005).
A novel mechanism of actin filament processive capping by formin: solution of the rotation paradox.
  J Cell Biol, 170, 889-893.  
15377785 D.R.Kovar, and T.D.Pollard (2004).
Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces.
  Proc Natl Acad Sci U S A, 101, 14725-14730.  
15242634 E.S.Harris, and H.N.Higgs (2004).
Actin cytoskeleton: formins lead the way.
  Curr Biol, 14, R520-R522.  
15256004 F.Cvrcková, M.Novotný, D.Pícková, and V.Zárský (2004).
Formin homology 2 domains occur in multiple contexts in angiosperms.
  BMC Genomics, 5, 44.  
15528434 J.Møller-Jensen, and K.Gerdes (2004).
Microbiology. Dynamic instability of a bacterial engine.
  Science, 306, 987-989.  
15371418 J.W.Copeland, S.J.Copeland, and R.Treisman (2004).
Homo-oligomerization is essential for F-actin assembly by the formin family FH2 domain.
  J Biol Chem, 279, 50250-50256.  
15362226 M.A.Wear, and J.A.Cooper (2004).
Capping protein: new insights into mechanism and regulation.
  Trends Biochem Sci, 29, 418-428.  
15466701 M.Bindschadler, and J.L.McGrath (2004).
Formin' new ideas about actin filament generation.
  Proc Natl Acad Sci U S A, 101, 14685-14686.  
15596547 M.M.Kozlov, and A.D.Bershadsky (2004).
Processive capping by formin suggests a force-driven mechanism of actin polymerization.
  J Cell Biol, 167, 1011-1017.  
15507212 S.Romero, C.Le Clainche, D.Didry, C.Egile, D.Pantaloni, and M.F.Carlier (2004).
Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis.
  Cell, 119, 419-429.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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