메뉴 건너뛰기




Volumn 19, Issue 8, 2012, Pages 754-759

Crystal structures of the JAK2 pseudokinase domain and the pathogenic mutant V617F

Author keywords

[No Author keywords available]

Indexed keywords

JANUS KINASE 2; SERINE; TYROSINE;

EID: 84864668290     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2348     Document Type: Article
Times cited : (187)

References (47)
  • 1
  • 2
    • 0036731485 scopus 로고    scopus 로고
    • Stats: Transcriptional control and biological impact
    • Levy, D.E. & Darnell, J.E. Jr. Stats: transcriptional control and biological impact. Nat. Rev. Mol. Cell Biol. 3, 651-662 (2002).
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 651-662
    • Levy, D.E.1    Darnell Jr., J.E.2
  • 3
    • 30144436273 scopus 로고    scopus 로고
    • The structural basis of Janus kinase 2 inhibition by a potent and specifc pan-Janus kinase inhibitor
    • Lucet, I.S. et al. The structural basis of Janus kinase 2 inhibition by a potent and specifc pan-Janus kinase inhibitor. Blood 107, 176-183 (2006).
    • (2006) Blood , vol.107 , pp. 176-183
    • Lucet, I.S.1
  • 4
    • 23044495944 scopus 로고    scopus 로고
    • Crystal structure of the Jak3 kinase domain in complex with a staurosporine analog
    • Boggon, T.J., Li, Y., Manley, P.W. & Eck, M.J. Crystal structure of the Jak3 kinase domain in complex with a staurosporine analog. Blood 106, 996-1002 (2005).
    • (2005) Blood , vol.106 , pp. 996-1002
    • Boggon, T.J.1    Li, Y.2    Manley, P.W.3    Eck, M.J.4
  • 5
    • 61349149899 scopus 로고    scopus 로고
    • Dissecting specifcity in the Janus kinases: The structures of JAK-specifc inhibitors complexed to the JAK1 and JAK2 protein tyrosine kinase domains
    • Williams, N.K. et al. Dissecting specifcity in the Janus kinases: the structures of JAK-specifc inhibitors complexed to the JAK1 and JAK2 protein tyrosine kinase domains. J. Mol. Biol. 387, 219-232 (2009).
    • (2009) J. Mol. Biol. , vol.387 , pp. 219-232
    • Williams, N.K.1
  • 6
    • 77954385114 scopus 로고    scopus 로고
    • Structural and thermodynamic characterization of the TYK2 and JAK3 kinase domains in complex with CP-690550 and CMP-6
    • Chrencik, J.E. et al. Structural and thermodynamic characterization of the TYK2 and JAK3 kinase domains in complex with CP-690550 and CMP-6. J. Mol. Biol. 400, 413-433 (2010).
    • (2010) J. Mol. Biol. , vol.400 , pp. 413-433
    • Chrencik, J.E.1
  • 7
    • 80051931772 scopus 로고    scopus 로고
    • New mutations and pathogenesis of myeloproliferative neoplasms
    • Vainchenker, W., Delhommeau, F., Constantinescu, S.N. & Bernard, O.A. New mutations and pathogenesis of myeloproliferative neoplasms. Blood 118, 1723-1735 (2011).
    • (2011) Blood , vol.118 , pp. 1723-1735
    • Vainchenker, W.1    Delhommeau, F.2    Constantinescu, S.N.3    Bernard, O.A.4
  • 8
    • 77953482860 scopus 로고    scopus 로고
    • Perspectives for the use of structural information and chemical genetics to develop inhibitors of Janus kinases
    • Haan, C., Behrmann, I. & Haan, S. Perspectives for the use of structural information and chemical genetics to develop inhibitors of Janus kinases. J. Cell. Mol. Med. 14, 504-527 (2010).
    • (2010) J. Cell. Mol. Med. , vol.14 , pp. 504-527
    • Haan, C.1    Behrmann, I.2    Haan, S.3
  • 9
    • 17644424955 scopus 로고    scopus 로고
    • A gain-of-function mutation of JAK2 in myeloproliferative disorders
    • Kralovics, R. et al. A gain-of-function mutation of JAK2 in myeloproliferative disorders. N. Engl. J. Med. 352, 1779-1790 (2005).
    • (2005) N. Engl. J. Med. , vol.352 , pp. 1779-1790
    • Kralovics, R.1
  • 10
    • 17844383458 scopus 로고    scopus 로고
    • A unique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera
    • James, C. et al. A unique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera. Nature 434, 1144-1148 (2005).
    • (2005) Nature , vol.434 , pp. 1144-1148
    • James, C.1
  • 11
    • 20144363192 scopus 로고    scopus 로고
    • Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders
    • Baxter, E.J. et al. Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders. Lancet 365, 1054-1061 (2005).
    • (2005) Lancet , vol.365 , pp. 1054-1061
    • Baxter, E.J.1
  • 12
    • 20244369569 scopus 로고    scopus 로고
    • Activating mutation in the tyrosine kinase JAK2 in polycythemia vera, essential thrombocythemia, and myeloid metaplasia with myelofbrosis
    • Levine, R.L. et al. Activating mutation in the tyrosine kinase JAK2 in polycythemia vera, essential thrombocythemia, and myeloid metaplasia with myelofbrosis. Cancer Cell 7, 387-397 (2005).
    • (2005) Cancer Cell , vol.7 , pp. 387-397
    • Levine, R.L.1
  • 13
    • 84862776857 scopus 로고    scopus 로고
    • Identifcation of new ALK and RET gene fusions from colorectal and lung cancer biopsies
    • Lipson, D. Identifcation of new ALK and RET gene fusions from colorectal and lung cancer biopsies. Nat. Med. 18, 382-384 (2012).
    • (2012) Nat. Med. , vol.18 , pp. 382-384
    • Lipson, D.1
  • 14
    • 0028857954 scopus 로고
    • Mutation of Jak3 in a patient with SCID: Essential role of Jak3 in lymphoid development
    • Russell, S.M. et al. Mutation of Jak3 in a patient with SCID: essential role of Jak3 in lymphoid development. Science 270, 797-800 (1995).
    • (1995) Science , vol.270 , pp. 797-800
    • Russell, S.M.1
  • 15
    • 0037033012 scopus 로고    scopus 로고
    • The pseudokinase domain is required for suppression of basal activity of Jak2 and Jak3 tyrosine kinases and for cytokine-inducible activation of signal transduction
    • Saharinen, P. & Silvennoinen, O. The pseudokinase domain is required for suppression of basal activity of Jak2 and Jak3 tyrosine kinases and for cytokine-inducible activation of signal transduction. J. Biol. Chem. 277, 47954-47963 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 47954-47963
    • Saharinen, P.1    Silvennoinen, O.2
  • 16
    • 0034012330 scopus 로고    scopus 로고
    • Regulation of the Jak2 tyrosine kinase by its pseudokinase domain
    • Saharinen, P., Takaluoma, K. & Silvennoinen, O. Regulation of the Jak2 tyrosine kinase by its pseudokinase domain. Mol. Cell. Biol. 20, 3387-3395 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3387-3395
    • Saharinen, P.1    Takaluoma, K.2    Silvennoinen, O.3
  • 17
    • 0033965488 scopus 로고    scopus 로고
    • Complex effects of naturally occurring mutations in the JAK3 pseudokinase domain: Evidence for interactions between the kinase and pseudokinase domains
    • Chen, M. et al. Complex effects of naturally occurring mutations in the JAK3 pseudokinase domain: evidence for interactions between the kinase and pseudokinase domains. Mol. Cell. Biol. 20, 947-956 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 947-956
    • Chen, M.1
  • 18
    • 0035045092 scopus 로고    scopus 로고
    • Prediction of the structure of human Janus kinase 2 (JAK2) comprising the two carboxy-terminal domains reveals a mechanism for autoregulation
    • Lindauer, K., Loerting, T., Liedl, K.R. & Kroemer, R.T. Prediction of the structure of human Janus kinase 2 (JAK2) comprising the two carboxy-terminal domains reveals a mechanism for autoregulation. Protein Eng. 14, 27-37 (2001).
    • (2001) Protein Eng , vol.14 , pp. 27-37
    • Lindauer, K.1    Loerting, T.2    Liedl, K.R.3    Kroemer, R.T.4
  • 19
    • 80052492285 scopus 로고    scopus 로고
    • The pseudokinase domain of JAK2 is a dual-specifcity protein kinase that negatively regulates cytokine signaling
    • Ungureanu, D. et al. The pseudokinase domain of JAK2 is a dual-specifcity protein kinase that negatively regulates cytokine signaling. Nat. Struct. Mol. Biol. 18, 971-976 (2011).
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 971-976
    • Ungureanu, D.1
  • 20
    • 0000127673 scopus 로고
    • 2.2 Å refned crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor
    • Zheng, J. et al. 2.2 Å refned crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor. Acta Crystallogr. D Biol. Crystallogr. 49, 362-365 (1993).
    • (1993) Acta Crystallogr. D Biol. Crystallogr. , vol.49 , pp. 362-365
    • Zheng, J.1
  • 21
    • 0030766163 scopus 로고    scopus 로고
    • Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog
    • Hubbard, S.R. Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J. 16, 5572-5581 (1997).
    • (1997) EMBO J , vol.16 , pp. 5572-5581
    • Hubbard, S.R.1
  • 22
    • 77952338791 scopus 로고    scopus 로고
    • ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation
    • Shi, F., Telesco, S.E., Liu, Y., Radhakrishnan, R. & Lemmon, M.A. ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation. Proc. Natl. Acad. Sci. USA 107, 7692-7697 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 7692-7697
    • Shi, F.1    Telesco, S.E.2    Liu, Y.3    Radhakrishnan, R.4    Lemmon, M.A.5
  • 23
    • 76049128717 scopus 로고    scopus 로고
    • Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3
    • Jura, N., Shan, Y., Cao, X., Shaw, D.E. & Kuriyan, J. Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3. Proc. Natl. Acad. Sci. USA 106, 21608-21613 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 21608-21613
    • Jura, N.1    Shan, Y.2    Cao, X.3    Shaw, D.E.4    Kuriyan, J.5
  • 24
    • 77955299093 scopus 로고    scopus 로고
    • JAK2 V617F constitutive activation requires JH2 residue F595: A pseudokinase domain target for specifc inhibitors
    • Dusa, A., Mouton, C., Pecquet, C., Herman, M. & Constantinescu, S.N. JAK2 V617F constitutive activation requires JH2 residue F595: a pseudokinase domain target for specifc inhibitors. PLoS ONE 5, e11157 (2010).
    • (2010) PLoS ONE , vol.5
    • Dusa, A.1    Mouton, C.2    Pecquet, C.3    Herman, M.4    Constantinescu, S.N.5
  • 25
    • 78649289718 scopus 로고    scopus 로고
    • The constitutive activation of Jak2-V617F is mediated by a π stacking mechanism involving phenylalanines 595 and 617
    • Gnanasambandan, K., Magis, A. & Sayeski, P.P. The constitutive activation of Jak2-V617F is mediated by a π stacking mechanism involving phenylalanines 595 and 617. Biochemistry 49, 9972-9984 (2010).
    • (2010) Biochemistry , vol.49 , pp. 9972-9984
    • Gnanasambandan, K.1    Magis, A.2    Sayeski, P.P.3
  • 26
    • 0033815252 scopus 로고    scopus 로고
    • Insights into nucleotide binding in protein kinase A using fuorescent adenosine derivatives
    • Ni, Q., Shaffer, J. & Adams, J.A. Insights into nucleotide binding in protein kinase A using fuorescent adenosine derivatives. Protein Sci. 9, 1818-1827 (2000).
    • (2000) Protein Sci , vol.9 , pp. 1818-1827
    • Ni, Q.1    Shaffer, J.2    Adams, J.A.3
  • 27
    • 2442637820 scopus 로고    scopus 로고
    • Autophosphorylation of JAK2 on tyrosines 221 and 570 regulates its activity
    • Argetsinger, L.S. et al. Autophosphorylation of JAK2 on tyrosines 221 and 570 regulates its activity. Mol. Cell. Biol. 24, 4955-4967 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4955-4967
    • Argetsinger, L.S.1
  • 28
    • 33646865516 scopus 로고    scopus 로고
    • Phosphorylation of Jak2 on Ser(523) inhibits Jak2-dependent leptin receptor signaling
    • Ishida-Takahashi, R. et al. Phosphorylation of Jak2 on Ser(523) inhibits Jak2-dependent leptin receptor signaling. Mol. Cell. Biol. 26, 4063-4073 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 4063-4073
    • Ishida-Takahashi, R.1
  • 29
    • 2442642830 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Jak2 in the JH2 domain inhibits cytokine signaling
    • Feener, E.P., Rosario, F., Dunn, S.L., Stancheva, Z. & Myers, M.G. Tyrosine phosphorylation of Jak2 in the JH2 domain inhibits cytokine signaling. Mol. Cell. Biol. 24, 4968-4978 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4968-4978
    • Feener, E.P.1    Rosario, F.2    Dunn, S.L.3    Stancheva, Z.4    Myers, M.G.5
  • 30
    • 33646864349 scopus 로고    scopus 로고
    • Phosphorylation of JAK2 at serine 523: A negative regulator of JAK2 that is stimulated by growth hormone and epidermal growth factor
    • Mazurkiewicz-Munoz, A.M. et al. Phosphorylation of JAK2 at serine 523: a negative regulator of JAK2 that is stimulated by growth hormone and epidermal growth factor. Mol. Cell. Biol. 26, 4052-4062 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 4052-4062
    • Mazurkiewicz-Munoz, A.M.1
  • 31
    • 70350351539 scopus 로고    scopus 로고
    • A JAK2 interdomain linker relays Epo receptor engagement signals to kinase activation
    • Zhao, L. et al. A JAK2 interdomain linker relays Epo receptor engagement signals to kinase activation. J. Biol. Chem. 284, 26988-26998 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 26988-26998
    • Zhao, L.1
  • 32
    • 0033548259 scopus 로고    scopus 로고
    • Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation
    • Livnah, O. et al. Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation. Science 283, 987-990 (1999).
    • (1999) Science , vol.283 , pp. 987-990
    • Livnah, O.1
  • 33
    • 84858855487 scopus 로고    scopus 로고
    • JAK inhibitors for myeloproliferative neoplasms: Clarifying facts from myths
    • Tefferi, A. JAK inhibitors for myeloproliferative neoplasms: clarifying facts from myths. Blood 119, 2721-2730 (2012).
    • (2012) Blood , vol.119 , pp. 2721-2730
    • Tefferi, A.1
  • 34
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. & Sander, C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637 (1983).
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A.A. & Teplyakov, A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30, 1022-1025 (1997).
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.A.1    Teplyakov, A.2
  • 39
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter, J. & Merritt, E.A. Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr. D Biol. Crystallogr. 62, 439-450 (2006).
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 40
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple Amber force felds and development of improved protein backbone parameters
    • Hornak, V. et al. Comparison of multiple Amber force felds and development of improved protein backbone parameters. Proteins 65, 712-725 (2006).
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1
  • 41
    • 77953513118 scopus 로고    scopus 로고
    • Improved side-chain torsion potentials for the Amber ff99SB protein force feld
    • Lindorff-Larsen, K. et al. Improved side-chain torsion potentials for the Amber ff99SB protein force feld. Proteins 78, 1950-1958 (2010).
    • (2010) Proteins , vol.78 , pp. 1950-1958
    • Lindorff-Larsen, K.1
  • 43
    • 84856878089 scopus 로고    scopus 로고
    • Millisecond-scale molecular dynamics simulations on anton
    • ACM
    • Shaw, D.E. et al. Millisecond-scale molecular dynamics simulations on Anton. in ACAM/IEEE Conference on Supercomputing (ACM, 2009).
    • (2009) ACAM IEEE Conference on Supercomputing
    • Shaw, D.E.1
  • 44
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • Hoover, W.G. Canonical dynamics: Equilibrium phase-space distributions. Phys. Rev. A 31, 1695-1697 (1985).
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 45
    • 33847728615 scopus 로고    scopus 로고
    • A common, avoidable source of error in molecular dynamics integrators
    • Lippert, R.A. et al. A common, avoidable source of error in molecular dynamics integrators. J. Chem. Phys. 126, 046101 (2007).
    • (2007) J. Chem. Phys. , vol.126 , pp. 046101
    • Lippert, R.A.1
  • 46
    • 0035871686 scopus 로고    scopus 로고
    • A fast SHAKE algorithm to solve distance constraint equations for small molecules in molecular dynamics simulations
    • Kräutler, V., Van Gunsteren, W.F. & Hunenberger, P.H. A fast SHAKE algorithm to solve distance constraint equations for small molecules in molecular dynamics simulations. J. Comput. Chem. 22, 501-508 (2001).
    • (2001) J. Comput. Chem. , vol.22 , pp. 501-508
    • Kräutler, V.1    Van Gunsteren, W.F.2    Hunenberger, P.H.3
  • 47
    • 33745299454 scopus 로고    scopus 로고
    • Is the Ewald summation still necessary? Pairwise alternatives to the accepted standard for long-range electrostatics
    • Fennell, C.J. & Gezelter, J.D. Is the Ewald summation still necessary? Pairwise alternatives to the accepted standard for long-range electrostatics. J. Chem. Phys. 124, 234104 (2006).
    • (2006) J. Chem. Phys. , vol.124 , pp. 234104
    • Fennell, C.J.1    Gezelter, J.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.