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PDBsum entry 2bfy
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protein ligands Protein-protein interface(s) links
Transferase PDB id
2bfy

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
272 a.a. *
39 a.a. *
34 a.a. *
Ligands
H1N ×2
Waters ×383
* Residue conservation analysis
PDB id:
2bfy
Name: Transferase
Title: Complex of aurora-b with incenp and hesperadin.
Structure: Aurora kinase b-a. Chain: a, b. Fragment: catalytic domain, residues 78-361. Synonym: loc398457 protein, aurora-b, aurora/ipl1-related kinase 2-a, airk2-a, xairk2-a, serine/threonine-protein kinase 12-a, serine/threonine-protein kinase aurora-b-a, xaurora-b. Engineered: yes. Mutation: yes. Other_details: phosphorylated on t248.
Source: Xenopus laevis. African clawed frog. Organism_taxid: 8355. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Biol. unit: Dimer (from PDB file)
Resolution:
1.80Å     R-factor:   0.203     R-free:   0.226
Authors: F.Sessa,M.Mapelli,C.Ciferri,C.Tarricone,L.B.Areces,T.R.Schneider, P.T.Stukenberg,A.Musacchio
Key ref:
F.Sessa et al. (2005). Mechanism of Aurora B activation by INCENP and inhibition by hesperadin. Mol Cell, 18, 379-391. PubMed id: 15866179 DOI: 10.1016/j.molcel.2005.03.031
Date:
15-Dec-04     Release date:   03-May-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q6DE08  (AUKBA_XENLA) -  Aurora kinase B-A from Xenopus laevis
Seq:
Struc: 		361 a.a.
272 a.a.*
Protein chain
Pfam   ArchSchema ?
O13024  (INCEA_XENLA) -  Inner centromere protein A from Xenopus laevis
Seq:
Struc: 		 
Seq:
Struc: 		873 a.a.
39 a.a.
Protein chain
Pfam   ArchSchema ?
O13024  (INCEA_XENLA) -  Inner centromere protein A from Xenopus laevis
Seq:
Struc: 		 
Seq:
Struc: 		873 a.a.
34 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.2.7.11.1  - non-specific serine/threonine protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
L-seryl-[protein]
 + ATP
 = O-phospho-L-seryl-[protein]
 + ADP
 + H(+)
L-threonyl-[protein]
 + ATP
 = O-phospho-L-threonyl-[protein]
 + ADP
 + H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1016/j.molcel.2005.03.031 Mol Cell 18:379-391 (2005)
PubMed id: 15866179  
 
 
Mechanism of Aurora B activation by INCENP and inhibition by hesperadin.
F.Sessa, M.Mapelli, C.Ciferri, C.Tarricone, L.B.Areces, T.R.Schneider, P.T.Stukenberg, A.Musacchio.
 
  ABSTRACT  
 
Aurora family serine/threonine kinases control mitotic progression, and their deregulation is implicated in tumorigenesis. Aurora A and Aurora B, the best-characterized members of mammalian Aurora kinases, are approximately 60% identical but bind to unrelated activating subunits. The structure of the complex of Aurora A with the TPX2 activator has been reported previously. Here, we report the crystal structure of Aurora B in complex with the IN-box segment of the inner centromere protein (INCENP) activator and with the small molecule inhibitor Hesperadin. The Aurora B:INCENP complex is remarkably different from the Aurora A:TPX2 complex. INCENP forms a crown around the small lobe of Aurora B and induces the active conformation of the T loop allosterically. The structure represents an intermediate state of activation of Aurora B in which the Aurora B C-terminal segment stabilizes an open conformation of the catalytic cleft, and a critical ion pair in the kinase active site is impaired. Phosphorylation of two serines in the carboxyl terminus of INCENP generates the fully active kinase.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. Details of the Aurora B:IN-box Interaction 		Figure 5.
Figure 5. Activation Mechanism of Aurora B
 
  The above figures are reprinted by permission from Cell Press: Mol Cell (2005, 18, 379-391) copyright 2005.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
23175282 M.Carmena, M.Wheelock, H.Funabiki, and W.C.Earnshaw (2012).
The chromosomal passenger complex (CPC): from easy rider to the godfather of mitosis.
  Nat Rev Mol Cell Biol, 13, 789-803.  
23064647 S.Hughes, F.Elustondo, A.Di Fonzo, F.G.Leroux, A.C.Wong, A.P.Snijders, S.J.Matthews, and P.Cherepanov (2012).
Crystal structure of human CDC7 kinase in complex with its activator DBF4.
  Nat Struct Mol Biol, 19, 1101-1107.
PDB codes: 4f99 4f9a 4f9b 4f9c
22796964 S.Liokatis, A.Stützer, S.J.Elsässer, F.X.Theillet, R.Klingberg, B.van Rossum, D.Schwarzer, C.D.Allis, W.Fischle, and P.Selenko (2012).
Phosphorylation of histone H3 Ser10 establishes a hierarchy for subsequent intramolecular modification events.
  Nat Struct Mol Biol, 19, 819-823.  
21106376 M.A.Lampson, and I.M.Cheeseman (2011).
Sensing centromere tension: Aurora B and the regulation of kinetochore function.
  Trends Cell Biol, 21, 133-140.  
  21554500 R.Ban, T.Nishida, and T.Urano (2011).
Mitotic kinase Aurora-B is regulated by SUMO-2/3 conjugation/deconjugation during mitosis.
  Genes Cells, 16, 652-669.  
20705815 A.E.Kelly, C.Ghenoiu, J.Z.Xue, C.Zierhut, H.Kimura, and H.Funabiki (2010).
Survivin reads phosphorylated histone H3 threonine 3 to activate the mitotic kinase Aurora B.
  Science, 330, 235-239.  
20181052 B.G.Fuller (2010).
Self-organization of intracellular gradients during mitosis.
  Cell Div, 5, 5.  
20067443 C.A.Dodson, M.Kosmopoulou, M.W.Richards, B.Atrash, V.Bavetsias, J.Blagg, and R.Bayliss (2010).
Crystal structure of an Aurora-A mutant that mimics Aurora-B bound to MLN8054: insights into selectivity and drug design.
  Biochem J, 427, 19-28.
PDB codes: 2wtv 2wtw
20663916 G.Fernández-Miranda, I.Pérez de Castro, M.Carmena, C.Aguirre-Portolés, S.Ruchaud, X.Fant, G.Montoya, W.C.Earnshaw, and M.Malumbres (2010).
SUMOylation modulates the function of Aurora-B kinase.
  J Cell Sci, 123, 2823-2833.  
20937697 J.C.Schmidt, T.Kiyomitsu, T.Hori, C.B.Backer, T.Fukagawa, and I.M.Cheeseman (2010).
Aurora B kinase controls the targeting of the Astrin-SKAP complex to bioriented kinetochores.
  J Cell Biol, 191, 269-280.  
20484572 K.T.Yang, S.K.Li, C.C.Chang, C.J.Tang, Y.N.Lin, S.C.Lee, and T.K.Tang (2010).
Aurora-C kinase deficiency causes cytokinesis failure in meiosis I and production of large polyploid oocytes in mice.
  Mol Biol Cell, 21, 2371-2383.  
21187329 K.Zeng, R.N.Bastos, F.A.Barr, and U.Gruneberg (2010).
Protein phosphatase 6 regulates mitotic spindle formation by controlling the T-loop phosphorylation state of Aurora A bound to its activator TPX2.
  J Cell Biol, 191, 1315-1332.  
19955215 L.J.Wilmeth, S.Shrestha, G.Montaño, J.Rashe, and C.B.Shuster (2010).
Mutual dependence of Mob1 and the chromosomal passenger complex for localization during mitosis.
  Mol Biol Cell, 21, 380-392.  
20921135 M.Posch, G.A.Khoudoli, S.Swift, E.M.King, J.G.Deluca, and J.R.Swedlow (2010).
Sds22 regulates aurora B activity and microtubule-kinetochore interactions at mitosis.
  J Cell Biol, 191, 61-74.  
  20044834 R.Krishnamurty, and D.J.Maly (2010).
Biochemical mechanisms of resistance to small-molecule protein kinase inhibitors.
  ACS Chem Biol, 5, 121-138.  
20562864 R.S.Nozawa, K.Nagao, H.T.Masuda, O.Iwasaki, T.Hirota, N.Nozaki, H.Kimura, and C.Obuse (2010).
Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms through Aurora B activation.
  Nat Cell Biol, 12, 719-727.  
20956539 Z.Xu, P.Vagnarelli, H.Ogawa, K.Samejima, and W.C.Earnshaw (2010).
Gradient of increasing Aurora B kinase activity is required for cells to execute mitosis.
  J Biol Chem, 285, 40163-40170.  
19185479 A.E.Kelly, and H.Funabiki (2009).
Correcting aberrant kinetochore microtubule attachments: an Aurora B-centric view.
  Curr Opin Cell Biol, 21, 51-58.  
19494039 F.Hans, D.A.Skoufias, S.Dimitrov, and R.L.Margolis (2009).
Molecular distinctions between Aurora A and B: a single residue change transforms Aurora A into correctly localized and functional Aurora B.
  Mol Biol Cell, 20, 3491-3502.  
19152640 H.Y.Wang, L.L.Li, Z.X.Cao, S.D.Luo, Y.Q.Wei, and S.Y.Yang (2009).
A Specific Pharmacophore Model of Aurora B Kinase Inhibitors and Virtual Screening Studies Based on it.
  Chem Biol Drug Des, 73, 115-126.  
20045785 J.A.Pérez Fidalgo, D.Roda, S.Roselló, E.Rodríguez-Braun, and A.Cervantes (2009).
Aurora kinase inhibitors: a new class of drugs targeting the regulatory mitotic system.
  Clin Transl Oncol, 11, 787-798.  
19918057 J.Eswaran, D.Patnaik, P.Filippakopoulos, F.Wang, R.L.Stein, J.W.Murray, J.M.Higgins, and S.Knapp (2009).
Structure and functional characterization of the atypical human kinase haspin.
  Proc Natl Acad Sci U S A, 106, 20198-20203.
PDB codes: 2vuw 3dlz 3iq7
19357306 J.Fu, M.Bian, J.Liu, Q.Jiang, and C.Zhang (2009).
A single amino acid change converts Aurora-A into Aurora-B-like kinase in terms of partner specificity and cellular function.
  Proc Natl Acad Sci U S A, 106, 6939-6944.  
19190331 J.H.DeMoe, S.Santaguida, J.R.Daum, A.Musacchio, and G.J.Gorbsky (2009).
A high throughput, whole cell screen for small molecule inhibitors of the mitotic spindle checkpoint identifies OM137, a novel Aurora kinase inhibitor.
  Cancer Res, 69, 1509-1516.  
19284385 K.Anderson, Z.Lai, O.B.McDonald, J.D.Stuart, E.N.Nartey, M.A.Hardwicke, K.Newlander, D.Dhanak, J.Adams, D.Patrick, R.A.Copeland, P.J.Tummino, and J.Yang (2009).
Biochemical characterization of GSK1070916, a potent and selective inhibitor of Aurora B and Aurora C kinases with an extremely long residence time1.
  Biochem J, 420, 259-265.  
18784935 L.J.Ahonen, A.M.Kukkonen, J.Pouwels, M.A.Bolton, C.D.Jingle, P.T.Stukenberg, and M.J.Kallio (2009).
Perturbation of Incenp function impedes anaphase chromatid movements and chromosomal passenger protein flux at centromeres.
  Chromosoma, 118, 71-84.  
19146389 L.Zhou, J.Li, R.George, S.Ruchaud, H.G.Zhou, J.E.Ladbury, W.C.Earnshaw, and X.Yuan (2009).
Effects of full-length borealin on the composition and protein-protein interaction activity of a binary chromosomal passenger complex.
  Biochemistry, 48, 1156-1161.  
19836940 M.Carmena, S.Ruchaud, and W.C.Earnshaw (2009).
Making the Auroras glow: regulation of Aurora A and B kinase function by interacting proteins.
  Curr Opin Cell Biol, 21, 796-805.  
19197328 M.Glotzer (2009).
The 3Ms of central spindle assembly: microtubules, motors and MAPs.
  Nat Rev Mol Cell Biol, 10, 9.  
19941817 M.W.Richards, L.O'Regan, C.Mas-Droux, J.M.Blot, J.Cheung, S.Hoelder, A.M.Fry, and R.Bayliss (2009).
An autoinhibitory tyrosine motif in the cell-cycle-regulated Nek7 kinase is released through binding of Nek9.
  Mol Cell, 36, 560-570.
PDB codes: 2wqm 2wqn 2wqo
19134008 M.Yasen, H.Mizushima, K.Mogushi, G.Obulhasim, K.Miyaguchi, K.Inoue, I.Nakahara, T.Ohta, A.Aihara, S.Tanaka, S.Arii, and H.Tanaka (2009).
Expression of Aurora B and alternative variant forms in hepatocellular carcinoma and adjacent tissue.
  Cancer Sci, 100, 472-480.  
19320832 N.Jetton, K.G.Rothberg, J.G.Hubbard, J.Wise, Y.Li, H.L.Ball, and L.Ruben (2009).
The cell cycle as a therapeutic target against Trypanosoma brucei: Hesperadin inhibits Aurora kinase-1 and blocks mitotic progression in bloodstream forms.
  Mol Microbiol, 72, 442-458.  
19359241 P.J.Scutt, M.L.Chu, D.A.Sloane, M.Cherry, C.R.Bignell, D.H.Williams, and P.A.Eyers (2009).
Discovery and exploitation of inhibitor-resistant aurora and polo kinase mutants for the analysis of mitotic networks.
  J Biol Chem, 284, 15880-15893.  
19995936 Y.Hayashi-Takanaka, K.Yamagata, N.Nozaki, and H.Kimura (2009).
Visualizing histone modifications in living cells: spatiotemporal dynamics of H3 phosphorylation during interphase.
  J Cell Biol, 187, 781-790.  
19951914 Z.Xu, H.Ogawa, P.Vagnarelli, J.H.Bergmann, D.F.Hudson, S.Ruchaud, T.Fukagawa, W.C.Earnshaw, and K.Samejima (2009).
INCENP-aurora B interactions modulate kinase activity and chromosome passenger complex localization.
  J Cell Biol, 187, 637-653.  
18574696 A.Poulsen, A.William, A.Lee, S.Blanchard, E.Teo, W.Deng, N.Tu, E.Tan, E.Sun, K.L.Goh, W.C.Ong, C.P.Ng, K.C.Goh, and Z.Bonday (2008).
Structure-based design of Aurora A & B inhibitors.
  J Comput Aided Mol Des, 22, 897-906.  
18068131 B.T.McGrogan, B.Gilmartin, D.N.Carney, and A.McCann (2008).
Taxanes, microtubules and chemoresistant breast cancer.
  Biochim Biophys Acta, 1785, 96.  
18455984 C.Ciferri, S.Pasqualato, E.Screpanti, G.Varetti, S.Santaguida, G.Dos Reis, A.Maiolica, J.Polka, J.G.De Luca, P.De Wulf, M.Salek, J.Rappsilber, C.A.Moores, E.D.Salmon, and A.Musacchio (2008).
Implications for kinetochore-microtubule attachment from the structure of an engineered Ndc80 complex.
  Cell, 133, 427-439.
PDB code: 2ve7
18334486 G.M.Riefler, S.Y.Dent, and J.M.Schumacher (2008).
Tousled-mediated activation of Aurora B kinase does not require Tousled kinase activity in vivo.
  J Biol Chem, 283, 12763-12768.  
18507820 G.Vader, A.F.Maia, and S.M.Lens (2008).
The chromosomal passenger complex and the spindle assembly checkpoint: kinetochore-microtubule error correction and beyond.
  Cell Div, 3, 10.  
18662747 G.Vader, and S.M.Lens (2008).
The Aurora kinase family in cell division and cancer.
  Biochim Biophys Acta, 1786, 60-72.  
18243099 N.Jelluma, A.B.Brenkman, N.J.van den Broek, C.W.Cruijsen, M.H.van Osch, S.M.Lens, R.H.Medema, and G.J.Kops (2008).
Mps1 phosphorylates Borealin to control Aurora B activity and chromosome alignment.
  Cell, 132, 233-246.  
18218899 S.E.Rosasco-Nitcher, W.Lan, S.Khorasanizadeh, and P.T.Stukenberg (2008).
Centromeric Aurora-B activation requires TD-60, microtubules, and substrate priming phosphorylation.
  Science, 319, 469-472.  
18249108 S.Taylor, and J.M.Peters (2008).
Polo and Aurora kinases: lessons derived from chemical biology.
  Curr Opin Cell Biol, 20, 77-84.  
18378691 T.M.Yamamoto, A.L.Lewellyn, and J.L.Maller (2008).
Regulation of the Aurora B chromosome passenger protein complex during oocyte maturation in Xenopus laevis.
  Mol Cell Biol, 28, 4196-4203.  
17956729 A.A.Jeyaprakash, U.R.Klein, D.Lindner, J.Ebert, E.A.Nigg, and E.Conti (2007).
Structure of a Survivin-Borealin-INCENP core complex reveals how chromosomal passengers travel together.
  Cell, 131, 271-285.
PDB code: 2qfa
17199039 A.E.Kelly, S.C.Sampath, T.A.Maniar, E.M.Woo, B.T.Chait, and H.Funabiki (2007).
Chromosomal enrichment and activation of the aurora B pathway are coupled to spatially regulate spindle assembly.
  Dev Cell, 12, 31-43.  
17765685 C.V.Kotwaliwale, S.B.Frei, B.M.Stern, and S.Biggins (2007).
A pathway containing the Ipl1/aurora protein kinase and the spindle midzone protein Ase1 regulates yeast spindle assembly.
  Dev Cell, 13, 433-445.  
17881355 E.Bourhis, S.G.Hymowitz, and A.G.Cochran (2007).
The mitotic regulator Survivin binds as a monomer to its functional interactor Borealin.
  J Biol Chem, 282, 35018-35023.
PDB codes: 2raw 2rax
17599067 F.Ikeda, C.M.Hecker, A.Rozenknop, R.D.Nordmeier, V.Rogov, K.Hofmann, S.Akira, V.Dötsch, and I.Dikic (2007).
Involvement of the ubiquitin-like domain of TBK1/IKK-i kinases in regulation of IFN-inducible genes.
  EMBO J, 26, 3451-3462.  
17240048 G.M.Cheetham, P.A.Charlton, J.M.Golec, and J.R.Pollard (2007).
Structural basis for potent inhibition of the Aurora kinases and a T315I multi-drug resistant mutant form of Abl kinase by VX-680.
  Cancer Lett, 251, 323-329.  
17699588 G.Vader, C.W.Cruijsen, T.van Harn, M.J.Vromans, R.H.Medema, and S.M.Lens (2007).
The chromosomal passenger complex controls spindle checkpoint function independent from its role in correcting microtubule kinetochore interactions.
  Mol Biol Cell, 18, 4553-4564.  
17500509 H.Al-Ali, T.J.Ragan, X.Gao, and T.K.Harris (2007).
Reconstitution of modular PDK1 functions on trans-splicing of the regulatory PH and catalytic kinase domains.
  Bioconjug Chem, 18, 1294-1302.  
18097415 K.Ramadan, R.Bruderer, F.M.Spiga, O.Popp, T.Baur, M.Gotta, and H.H.Meyer (2007).
Cdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin.
  Nature, 450, 1258-1262.  
17848966 S.Ruchaud, M.Carmena, and W.C.Earnshaw (2007).
Chromosomal passengers: conducting cell division.
  Nat Rev Mol Cell Biol, 8, 798-812.  
17942600 V.Pavicic-Kaltenbrunner, M.Mishima, and M.Glotzer (2007).
Cooperative assembly of CYK-4/MgcRacGAP and ZEN-4/MKLP1 to form the centralspindlin complex.
  Mol Biol Cell, 18, 4992-5003.  
16533707 A.G.Inche, and N.B.La Thangue (2006).
Chromatin control and cancer-drug discovery: realizing the promise.
  Drug Discov Today, 11, 97.  
16803889 A.Marx, C.Nugoor, J.Müller, S.Panneerselvam, T.Timm, M.Bilang, E.Mylonas, D.I.Svergun, E.M.Mandelkow, and E.Mandelkow (2006).
Structural variations in the catalytic and ubiquitin-associated domains of microtubule-associated protein/microtubule affinity regulating kinase (MARK) 1 and MARK2.
  J Biol Chem, 281, 27586-27599.
PDB code: 2hak
17087760 D.Kurihara, S.Matsunaga, A.Kawabe, S.Fujimoto, M.Noda, S.Uchiyama, and K.Fukui (2006).
Aurora kinase is required for chromosome segregation in tobacco BY-2 cells.
  Plant J, 48, 572-580.  
16769825 G.Vader, R.H.Medema, and S.M.Lens (2006).
The chromosomal passenger complex: guiding Aurora-B through mitosis.
  J Cell Biol, 173, 833-837.  
17070031 J.F.Couture, and R.C.Trievel (2006).
Histone-modifying enzymes: encrypting an enigmatic epigenetic code.
  Curr Opin Struct Biol, 16, 753-760.  
16407408 J.Rosa, P.Canovas, A.Islam, D.C.Altieri, and S.J.Doxsey (2006).
Survivin modulates microtubule dynamics and nucleation throughout the cell cycle.
  Mol Biol Cell, 17, 1483-1493.  
16499958 L.Penengo, M.Mapelli, A.G.Murachelli, S.Confalonieri, L.Magri, A.Musacchio, P.P.Di Fiore, S.Polo, and T.R.Schneider (2006).
Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin.
  Cell, 124, 1183-1195.
PDB codes: 2c7m 2c7n
17084073 M.G.Gold, D.Barford, and D.Komander (2006).
Lining the pockets of kinases and phosphatases.
  Curr Opin Struct Biol, 16, 693-701.  
16375648 N.Matthews, C.Visintin, B.Hartzoulakis, A.Jarvis, and D.L.Selwood (2006).
Aurora A and B kinases as targets for cancer: will they be selective for tumors?
  Expert Rev Anticancer Ther, 6, 109-120.  
16765893 R.R.Wei, J.R.Schnell, N.A.Larsen, P.K.Sorger, J.J.Chou, and S.C.Harrison (2006).
Structure of a central component of the yeast kinetochore: the Spc24p/Spc25p globular domain.
  Structure, 14, 1003-1009.
PDB code: 2fv4
16441230 S.Fu, W.Hu, J.J.Kavanagh, and R.C.Bast (2006).
Targeting Aurora kinases in ovarian cancer.
  Expert Opin Ther Targets, 10, 77-85.  
16785988 S.Ohashi, G.Sakashita, R.Ban, M.Nagasawa, H.Matsuzaki, Y.Murata, H.Taniguchi, H.Shima, K.Furukawa, and T.Urano (2006).
Phospho-regulation of human protein kinase Aurora-A: analysis using anti-phospho-Thr288 monoclonal antibodies.
  Oncogene, 25, 7691-7702.  
17174893 S.Sandall, F.Severin, I.X.McLeod, J.R.Yates, K.Oegema, A.Hyman, and A.Desai (2006).
A Bir1-Sli15 complex connects centromeres to microtubules and is required to sense kinetochore tension.
  Cell, 127, 1179-1191.  
16571674 U.R.Klein, E.A.Nigg, and U.Gruneberg (2006).
Centromere targeting of the chromosomal passenger complex requires a ternary subcomplex of Borealin, Survivin, and the N-terminal domain of INCENP.
  Mol Biol Cell, 17, 2547-2558.  
17085044 Z.Shi, K.A.Resing, and N.G.Ahn (2006).
Networks for the allosteric control of protein kinases.
  Curr Opin Struct Biol, 16, 686-692.  
16199877 H.K.Huang, J.M.Bailis, J.D.Leverson, E.B.Gómez, S.L.Forsburg, and T.Hunter (2005).
Suppressors of Bir1p (Survivin) identify roles for the chromosomal passenger protein Pic1p (INCENP) and the replication initiation factor Psf2p in chromosome segregation.
  Mol Cell Biol, 25, 9000-9015.  
16222244 T.Hirota, J.J.Lipp, B.H.Toh, and J.M.Peters (2005).
Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin.
  Nature, 438, 1176-1180.  
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 codes are shown on the right.

 

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