PDBsum entry 1khx

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protein links
Transcription PDB id
Protein chain
203 a.a. *
Waters ×144
* Residue conservation analysis
PDB id:
Name: Transcription
Title: Crystal structure of a phosphorylated smad2
Structure: Smad2. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Trimer (from PDB file)
1.80Å     R-factor:   0.215     R-free:   0.241
Authors: J.-W.Wu,M.Hu,J.Chai,J.Seoane,M.Huse,S.Kyin,T.W.Muir,R.Fairma J.Massague,Y.Shi
Key ref:
J.W.Wu et al. (2001). Crystal structure of a phosphorylated Smad2. Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling. Mol Cell, 8, 1277-1289. PubMed id: 11779503 DOI: 10.1016/S1097-2765(01)00421-X
01-Dec-01     Release date:   06-Feb-02    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q15796  (SMAD2_HUMAN) -  Mothers against decapentaplegic homolog 2
467 a.a.
203 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     intracellular   1 term 
  Biological process     regulation of transcription, DNA-dependent   1 term 


DOI no: 10.1016/S1097-2765(01)00421-X Mol Cell 8:1277-1289 (2001)
PubMed id: 11779503  
Crystal structure of a phosphorylated Smad2. Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling.
J.W.Wu, M.Hu, J.Chai, J.Seoane, M.Huse, C.Li, D.J.Rigotti, S.Kyin, T.W.Muir, R.Fairman, J.Massagué, Y.Shi.
Ligand-induced phosphorylation of the receptor-regulated Smads (R-Smads) is essential in the receptor Ser/Thr kinase-mediated TGF-beta signaling. The crystal structure of a phosphorylated Smad2, at 1.8 A resolution, reveals the formation of a homotrimer mediated by the C-terminal phosphoserine (pSer) residues. The pSer binding surface on the MH2 domain, frequently targeted for inactivation in cancers, is highly conserved among the Co- and R-Smads. This finding, together with mutagenesis data, pinpoints a functional interface between Smad2 and Smad4. In addition, the pSer binding surface on the MH2 domain coincides with the surface on R-Smads that is required for docking interactions with the serine-phosphorylated receptor kinases. These observations define a bifunctional role for the MH2 domain as a pSer-X-pSer binding module in receptor Ser/Thr kinase signaling pathways.
  Selected figure(s)  
Figure 4.
Figure 4. A Close-Up View of the Interactions between the Phosphorylated C Terminus from One Monomer and the Loop-Strand Pocket of the Adjacent Monomer(A) An electron density map of the phosphorylated C terminus. The 2F[o]-F[c] map (omit map), shown in pink, was contoured at 1.5σ and was calculated by simulated annealing using CNS (Brunger et al., 1998) with the omission of the C-terminal five residues. The backbone as well as the side chains of four residues are shown in yellow.(B) An overall view of the interactions. The C terminus is shown as a yellow coil, while its binding partner is represented as a transparent surface with backbones in pink. The side chains of the last five residues in the C terminus (CSSMS) and the basic residues in the loop-strand pocket are shown.(C) A stereo view of hydrogen bond networks. The two interacting monomers are shown in green and blue, respectively. Their side chains are colored gold and yellow. Hydrogen bonds among oxygen (red) and nitrogen (blue) atoms and water molecules (red) are indicated by red dashed lines.(D) A stereo view of the van der Waals contacts between the phosphorylated C terminus from one monomer and the loop-strand pocket of the adjacent monomer. The coloring scheme is the same as in (C).
Figure 6.
Figure 6. Implications for RSK-Mediated Signaling(A) Proposed mechanisms of Smad2 dissociation from the receptor kinase (TβRI) (Huse et al., 1999) after phosphorylation. The positively charged loop-strand pocket on Smad2, which is responsible for binding the phosphorylated C terminus of another Smad2, coincides with the L3 loop region, which is involved in interactions with the L45 loop and the GS region of the receptor kinase. The mutual exclusion is proposed to lead to dissociation of phosphorylated Smad2 from the receptors.(B) A schematic diagram of signal flow in the RSK-mediated signaling, highlighting the MH2 domain as the pSer binding motif.
  The above figures are reprinted by permission from Cell Press: Mol Cell (2001, 8, 1277-1289) copyright 2001.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21050181 D.Su, X.Peng, S.Zhu, Y.Huang, Z.Dong, Y.Zhang, J.Zhang, Q.Liang, J.Lu, and B.Huang (2010).
Role of p38 MAPK pathway in BMP4-mediated Smad-dependent premature senescence in lung cancer cells.
  Biochem J, 433, 333-343.  
20946979 M.Vila-Perelló, and T.W.Muir (2010).
Biological applications of protein splicing.
  Cell, 143, 191-200.  
20147459 N.BabuRajendran, P.Palasingam, K.Narasimhan, W.Sun, S.Prabhakar, R.Jauch, and P.R.Kolatkar (2010).
Structure of Smad1 MH1/DNA complex reveals distinctive rearrangements of BMP and TGF-beta effectors.
  Nucleic Acids Res, 38, 3477-3488.
PDB code: 3kmp
20922740 S.Möcklinghoff, R.Rose, M.Carraz, A.Visser, C.Ottmann, and L.Brunsveld (2010).
Synthesis and crystal structure of a phosphorylated estrogen receptor ligand binding domain.
  Chembiochem, 11, 2251-2254.
PDB codes: 3oll 3ols
20923499 S.N.Yang, M.L.Burch, L.R.Tannock, S.Evanko, N.Osman, and P.J.Little (2010).
Transforming growth factor-β regulation of proteoglycan synthesis in vascular smooth muscle: contribution to lipid binding and accelerated atherosclerosis in diabetes.
  J Diabetes, 2, 233-242.  
19458083 C.Millet, M.Yamashita, M.Heller, L.R.Yu, T.D.Veenstra, and Y.E.Zhang (2009).
A negative feedback control of transforming growth factor-beta signaling by glycogen synthase kinase 3-mediated Smad3 linker phosphorylation at Ser-204.
  J Biol Chem, 284, 19808-19816.  
19114992 C.S.Hill (2009).
Nucleocytoplasmic shuttling of Smad proteins.
  Cell Res, 19, 36-46.  
19557331 C.Wang, L.Chen, L.Wang, and J.Wu (2009).
Crystal structure of the MH2 domain of Drosophila Mad.
  Sci China C Life Sci, 52, 539-544.
PDB code: 3gmj
19223462 D.C.Clarke, M.L.Brown, R.A.Erickson, Y.Shi, and X.Liu (2009).
Transforming growth factor beta depletion is the primary determinant of Smad signaling kinetics.
  Mol Cell Biol, 29, 2443-2455.  
  19308291 D.P.Simon, S.Vadakkadath Meethal, A.C.Wilson, M.J.Gallego, S.L.Weinecke, E.Bruce, P.F.Lyons, R.J.Haasl, R.L.Bowen, and C.S.Atwood (2009).
Activin receptor signaling regulates prostatic epithelial cell adhesion and viability.
  Neoplasia, 11, 365-376.  
19855015 P.Kahlem, and S.J.Newfeld (2009).
Informatics approaches to understanding TGFbeta pathway regulation.
  Development, 136, 3729-3740.  
19254534 S.W.Chung, F.L.Miles, R.A.Sikes, C.R.Cooper, M.C.Farach-Carson, and B.A.Ogunnaike (2009).
Quantitative modeling and analysis of the transforming growth factor beta signaling pathway.
  Biophys J, 96, 1733-1750.  
18332103 A.Lonic, E.F.Barry, C.Quach, B.Kobe, N.Saunders, and M.A.Guthridge (2008).
Fibroblast growth factor receptor 2 phosphorylation on serine 779 couples to 14-3-3 and regulates cell survival and proliferation.
  Mol Cell Biol, 28, 3372-3385.  
18797952 C.E.Konikoff, R.G.Wisotzkey, and S.J.Newfeld (2008).
Lysine conservation and context in TGFbeta and Wnt signaling suggest new targets and general themes for posttranslational modification.
  J Mol Evol, 67, 323-333.  
18948271 J.Li, I.A.Taylor, J.Lloyd, J.A.Clapperton, S.Howell, D.Macmillan, and S.J.Smerdon (2008).
  J Biol Chem, 283, 36019-36030.  
18595660 M.Hirota, K.Watanabe, S.Hamada, Y.Sun, L.Strizzi, M.Mancino, T.Nagaoka, M.Gonzales, M.Seno, C.Bianco, and D.S.Salomon (2008).
Smad2 functions as a co-activator of canonical Wnt/beta-catenin signaling pathway independent of Smad4 through histone acetyltransferase activity of p300.
  Cell Signal, 20, 1632-1641.  
  18997322 R.Hao, L.Chen, J.W.Wu, and Z.X.Wang (2008).
Structure of Drosophila Mad MH2 domain.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 986-990.
PDB code: 3dit
18175316 R.Hariharan, and M.R.Pillai (2008).
Structure-function relationship of inhibitory Smads: Structural flexibility contributes to functional divergence.
  Proteins, 71, 1853-1862.  
19081050 S.Pennell, and S.J.Smerdon (2008).
Pellino proteins splitting up the FHAmily!
  Structure, 16, 1752-1754.  
18061509 S.Ross, and C.S.Hill (2008).
How the Smads regulate transcription.
  Int J Biochem Cell Biol, 40, 383-408.  
18924136 T.W.Muir (2008).
Studying protein structure and function using semisynthesis.
  Biopolymers, 90, 743-750.  
18836453 W.Chen, S.S.Lam, H.Srinath, Z.Jiang, J.J.Correia, C.A.Schiffer, K.A.Fitzgerald, K.Lin, and W.E.Royer (2008).
Insights into interferon regulatory factor activation from the crystal structure of dimeric IRF5.
  Nat Struct Mol Biol, 15, 1213-1220.
PDB code: 3dsh
18160410 W.Gong, D.Zhou, Y.Ren, Y.Wang, Z.Zuo, Y.Shen, F.Xiao, Q.Zhu, A.Hong, X.Zhou, X.Gao, and T.Li (2008).
PepCyber:P~PEP: a database of human protein protein interactions mediated by phosphoprotein-binding domains.
  Nucleic Acids Res, 36, D679-D683.  
  16858008 B.Hu, Z.Wu, T.Liu, M.R.Ullenbruch, H.Jin, and S.H.Phan (2007).
Gut-enriched Krüppel-like factor interaction with Smad3 inhibits myofibroblast differentiation.
  Am J Respir Cell Mol Biol, 36, 78-84.  
17195266 D.Rauh, and H.Waldmann (2007).
Linking chemistry and biology for the study of protein function.
  Angew Chem Int Ed Engl, 46, 826-829.  
17289590 G.Sapkota, C.Alarcón, F.M.Spagnoli, A.H.Brivanlou, and J.Massagué (2007).
Balancing BMP signaling through integrated inputs into the Smad1 linker.
  Mol Cell, 25, 441-454.  
18006160 K.V.Gromova, M.Friedrich, A.Noskov, and G.S.Harms (2007).
Visualizing Smad1/4 signaling response to bone morphogenetic protein-4 activation by FRET biosensors.
  Biochim Biophys Acta, 1773, 1759-1773.  
17785517 L.Xu, X.Yao, X.Chen, P.Lu, B.Zhang, and Y.T.Ip (2007).
Msk is required for nuclear import of TGF-{beta}/BMP-activated Smads.
  J Cell Biol, 178, 981-994.  
17140726 T.F.Lerch, M.Xu, T.S.Jardetzky, K.E.Mayo, I.Radhakrishnan, R.Kazer, L.D.Shea, and T.K.Woodruff (2007).
The structures that underlie normal reproductive function.
  Mol Cell Endocrinol, 267, 1-5.  
17283070 W.Chen, S.S.Lam, H.Srinath, C.A.Schiffer, W.E.Royer, and K.Lin (2007).
Competition between Ski and CREB-binding protein for binding to Smad proteins in transforming growth factor-beta signaling.
  J Biol Chem, 282, 11365-11376.  
17923090 X.Tang, J.S.Gao, Y.J.Guan, K.E.McLane, Z.L.Yuan, B.Ramratnam, and Y.E.Chin (2007).
Acetylation-dependent signal transduction for type I interferon receptor.
  Cell, 131, 93.  
16862174 Y.Inoue, Y.Itoh, K.Abe, T.Okamoto, H.Daitoku, A.Fukamizu, K.Onozaki, and H.Hayashi (2007).
Smad3 is acetylated by p300/CBP to regulate its transactivation activity.
  Oncogene, 26, 500-508.  
16449645 A.Kurisaki, K.Kurisaki, M.Kowanetz, H.Sugino, Y.Yoneda, C.H.Heldin, and A.Moustakas (2006).
The mechanism of nuclear export of Smad3 involves exportin 4 and Ran.
  Mol Cell Biol, 26, 1318-1332.  
16829979 B.T.Seet, I.Dikic, M.M.Zhou, and T.Pawson (2006).
Reading protein modifications with interaction domains.
  Nat Rev Mol Cell Biol, 7, 473-483.  
16377642 L.Tang, S.Breinig, L.Stith, A.Mischel, J.Tannir, B.Kokona, R.Fairman, and E.K.Jaffe (2006).
Single amino acid mutations alter the distribution of human porphobilinogen synthase quaternary structure isoforms (morpheeins).
  J Biol Chem, 281, 6682-6690.  
16437163 M.A.Guthridge, J.A.Powell, E.F.Barry, F.C.Stomski, B.J.McClure, H.Ramshaw, F.A.Felquer, M.Dottore, D.T.Thomas, B.To, C.G.Begley, and A.F.Lopez (2006).
Growth factor pleiotropy is controlled by a receptor Tyr/Ser motif that acts as a binary switch.
  EMBO J, 25, 479-489.  
17132729 S.K.Lim, and F.M.Hoffmann (2006).
Smad4 cooperates with lymphoid enhancer-binding factor 1/T cell-specific factor to increase c-myc expression in the absence of TGF-beta signaling.
  Proc Natl Acad Sci U S A, 103, 18580-18585.  
16721376 V.Muralidharan, and T.W.Muir (2006).
Protein ligation: an enabling technology for the biophysical analysis of proteins.
  Nat Methods, 3, 429-438.  
16751102 W.He, D.C.Dorn, H.Erdjument-Bromage, P.Tempst, M.A.Moore, and J.Massagué (2006).
Hematopoiesis controlled by distinct TIF1gamma and Smad4 branches of the TGFbeta pathway.
  Cell, 125, 929-941.  
16751101 X.Lin, X.Duan, Y.Y.Liang, Y.Su, K.H.Wrighton, J.Long, M.Hu, C.M.Davis, J.Wang, F.C.Brunicardi, Y.Shi, Y.G.Chen, A.Meng, and X.H.Feng (2006).
PPM1A functions as a Smad phosphatase to terminate TGFbeta signaling.
  Cell, 125, 915-928.  
15817471 A.Morén, T.Imamura, K.Miyazono, C.H.Heldin, and A.Moustakas (2005).
Degradation of the tumor suppressor Smad4 by WW and HECT domain ubiquitin ligases.
  J Biol Chem, 280, 22115-22123.  
15576564 B.A.Joughin, B.Tidor, and M.B.Yaffe (2005).
A computational method for the analysis and prediction of protein:phosphopeptide-binding sites.
  Protein Sci, 14, 131-139.  
16154084 B.Y.Qin, C.Liu, H.Srinath, S.S.Lam, J.J.Correia, R.Derynck, and K.Lin (2005).
Crystal structure of IRF-3 in complex with CBP.
  Structure, 13, 1269-1277.  
15799969 H.B.Chen, J.G.Rud, K.Lin, and L.Xu (2005).
Nuclear targeting of transforming growth factor-beta-activated Smad complexes.
  J Biol Chem, 280, 21329-21336.  
16109720 S.Gao, J.Steffen, and A.Laughon (2005).
Dpp-responsive silencers are bound by a trimeric Mad-Medea complex.
  J Biol Chem, 280, 36158-36164.  
15994459 V.Prokova, S.Mavridou, P.Papakosta, and D.Kardassis (2005).
Characterization of a novel transcriptionally active domain in the transforming growth factor beta-regulated Smad3 protein.
  Nucleic Acids Res, 33, 3708-3721.  
15632116 W.Zheng, D.Schwarzer, A.Lebeau, J.L.Weller, D.C.Klein, and P.A.Cole (2005).
Cellular stability of serotonin N-acetyltransferase conferred by phosphonodifluoromethylene alanine (Pfa) substitution for Ser-205.
  J Biol Chem, 280, 10462-10467.  
16212511 X.H.Feng, and R.Derynck (2005).
Specificity and versatility in tgf-beta signaling through Smads.
  Annu Rev Cell Dev Biol, 21, 659-693.  
15210694 I.Yakymovych, C.H.Heldin, and S.Souchelnytskyi (2004).
Smad2 phosphorylation by type I receptor: contribution of arginine 462 and cysteine 463 In the C terminus of Smad2 for specificity.
  J Biol Chem, 279, 35781-35787.  
14993291 J.P.Frederick, N.T.Liberati, D.S.Waddell, Y.Shi, and X.F.Wang (2004).
Transforming growth factor beta-mediated transcriptional repression of c-myc is dependent on direct binding of Smad3 to a novel repressive Smad binding element.
  Mol Cell Biol, 24, 2546-2559.  
14991001 L.Xu, and J.Massagué (2004).
Nucleocytoplasmic shuttling of signal transducers.
  Nat Rev Mol Cell Biol, 5, 209-219.  
15139812 M.B.Yaffe, and S.J.Smerdon (2004).
The use of in vitro peptide-library screens in the analysis of phosphoserine/threonine-binding domain structure and function.
  Annu Rev Biophys Biomol Struct, 33, 225-244.  
15523718 M.E.Hahn, and T.W.Muir (2004).
Photocontrol of Smad2, a multiphosphorylated cell-signaling protein, through caging of activating phosphoserines.
  Angew Chem Int Ed Engl, 43, 5800-5803.  
14720321 M.Kondo, H.Suzuki, K.Takehara, K.Miyazono, and M.Kato (2004).
Transforming growth factor-beta signaling is differentially inhibited by Smad2D450E and Smad3D407E.
  Cancer Sci, 95, 12-17.  
14729957 R.A.Randall, M.Howell, C.S.Page, A.Daly, P.A.Bates, and C.S.Hill (2004).
Recognition of phosphorylated-Smad2-containing complexes by a novel Smad interaction motif.
  Mol Cell Biol, 24, 1106-1121.  
12794086 A.Morén, U.Hellman, Y.Inada, T.Imamura, C.H.Heldin, and A.Moustakas (2003).
Differential ubiquitination defines the functional status of the tumor suppressor Smad4.
  J Biol Chem, 278, 33571-33582.  
14555996 B.Y.Qin, C.Liu, S.S.Lam, H.Srinath, R.Delston, J.J.Correia, R.Derynck, and K.Lin (2003).
Crystal structure of IRF-3 reveals mechanism of autoinhibition and virus-induced phosphoactivation.
  Nat Struct Biol, 10, 913-921.
PDB code: 1qwt
12700238 E.Dumont, F.Lallemand, C.Prunier, N.Ferrand, A.Guillouzo, B.Clément, A.Atfi, and N.Théret (2003).
Evidence for a role of Smad3 and Smad2 in stabilization of the tumor-derived mutant Smad2.Q407R.
  J Biol Chem, 278, 24881-24887.  
14500786 G.I.Lee, Z.Ding, J.C.Walker, and S.R.Van Doren (2003).
NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase.
  Proc Natl Acad Sci U S A, 100, 11261-11266.
PDB codes: 1mzk 1n4t
12824914 K.Miyazono, H.Suzuki, and T.Imamura (2003).
Regulation of TGF-beta signaling and its roles in progression of tumors.
  Cancer Sci, 94, 230-234.  
14555995 K.Takahasi, N.N.Suzuki, M.Horiuchi, M.Mori, W.Suhara, Y.Okabe, Y.Fukuhara, H.Terasawa, S.Akira, T.Fujita, and F.Inagaki (2003).
X-ray crystal structure of IRF-3 and its functional implications.
  Nat Struct Biol, 10, 922-927.
PDB code: 1j2f
12917407 L.Xu, C.Alarcón, S.Cöl, and J.Massagué (2003).
Distinct domain utilization by Smad3 and Smad4 for nucleoporin interaction and nuclear import.
  J Biol Chem, 278, 42569-42577.  
12426322 M.Mizuide, T.Hara, T.Furuya, M.Takeda, K.Kusanagi, Y.Inada, M.Mori, T.Imamura, K.Miyazawa, and K.Miyazono (2003).
Two short segments of Smad3 are important for specific interaction of Smad3 with c-Ski and SnoN.
  J Biol Chem, 278, 531-536.  
14557817 P.M.Siegel, and J.Massagué (2003).
Cytostatic and apoptotic actions of TGF-beta in homeostasis and cancer.
  Nat Rev Cancer, 3, 807-821.  
14534577 R.Derynck, and Y.E.Zhang (2003).
Smad-dependent and Smad-independent pathways in TGF-beta family signalling.
  Nature, 425, 577-584.  
12897770 S.Breinig, J.Kervinen, L.Stith, A.S.Wasson, R.Fairman, A.Wlodawer, A.Zdanov, and E.K.Jaffe (2003).
Control of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase.
  Nat Struct Biol, 10, 757-763.
PDB code: 1pv8
12702867 T.Pawson, and P.Nash (2003).
Assembly of cell regulatory systems through protein interaction domains.
  Science, 300, 445-452.  
12626339 T.W.Muir (2003).
Semisynthesis of proteins by expressed protein ligation.
  Annu Rev Biochem, 72, 249-289.  
12581521 X.Zheng, J.Wang, T.E.Haerry, A.Y.Wu, J.Martin, M.B.O'Connor, C.H.Lee, and T.Lee (2003).
TGF-beta signaling activates steroid hormone receptor expression during neuronal remodeling in the Drosophila brain.
  Cell, 112, 303-315.  
12809600 Y.Shi, and J.Massagué (2003).
Mechanisms of TGF-beta signaling from cell membrane to the nucleus.
  Cell, 113, 685-700.  
12468540 Z.Zhang, K.Shen, W.Lu, and P.A.Cole (2003).
The role of C-terminal tyrosine phosphorylation in the regulation of SHP-1 explored via expressed protein ligation.
  J Biol Chem, 278, 4668-4674.  
12440701 A.Mehra, and J.L.Wrana (2002).
TGF-beta and the Smad signal transduction pathway.
  Biochem Cell Biol, 80, 605-622.  
12154125 B.Y.Qin, S.S.Lam, J.J.Correia, and K.Lin (2002).
Smad3 allostery links TGF-beta receptor kinase activation to transcriptional control.
  Genes Dev, 16, 1950-1963.
PDB codes: 1mjs 1mk2
12374795 G.J.Inman, and C.S.Hill (2002).
Stoichiometry of active smad-transcription factor complexes on DNA.
  J Biol Chem, 277, 51008-51016.  
12191474 G.J.Inman, F.J.Nicolás, and C.S.Hill (2002).
Nucleocytoplasmic shuttling of Smads 2, 3, and 4 permits sensing of TGF-beta receptor activity.
  Mol Cell, 10, 283-294.  
11796104 J.L.Wrana (2002).
Phosphoserine-dependent regulation of protein-protein interactions in the Smad pathway.
  Structure, 10, 5-7.  
12419246 J.W.Wu, A.R.Krawitz, J.Chai, W.Li, F.Zhang, K.Luo, and Y.Shi (2002).
Structural mechanism of Smad4 recognition by the nuclear oncoprotein Ski: insights on Ski-mediated repression of TGF-beta signaling.
  Cell, 111, 357-367.
PDB code: 1mr1
12485160 K.Miyazawa, M.Shinozaki, T.Hara, T.Furuya, and K.Miyazono (2002).
Two major Smad pathways in TGF-beta superfamily signalling.
  Genes Cells, 7, 1191-1204.  
12191473 L.Xu, Y.Kang, S.Cöl, and J.Massagué (2002).
Smad2 nucleocytoplasmic shuttling by nucleoporins CAN/Nup214 and Nup153 feeds TGFbeta signaling complexes in the cytoplasm and nucleus.
  Mol Cell, 10, 271-282.  
12323349 R.M.Hofmann, and T.W.Muir (2002).
Recent advances in the application of expressed protein ligation to protein engineering.
  Curr Opin Biotechnol, 13, 297-303.  
12185845 S.Souchelnytskyi, A.Moustakas, and C.H.Heldin (2002).
TGF-beta signaling from a three-dimensional perspective: insight into selection of partners.
  Trends Cell Biol, 12, 304-307.  
12024051 X.Xu, L.M.Tsvetkov, and D.F.Stern (2002).
Chk2 activation and phosphorylation-dependent oligomerization.
  Mol Cell Biol, 22, 4419-4432.  
12023967 Z.J.Shen, T.Nakamoto, K.Tsuji, A.Nifuji, K.Miyazono, T.Komori, H.Hirai, and M.Noda (2002).
Negative regulation of bone morphogenetic protein/Smad signaling by Cas-interacting zinc finger protein in osteoblasts.
  J Biol Chem, 277, 29840-29846.  
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.