메뉴 건너뛰기




Volumn 6, Issue 10, 1998, Pages 1279-1290

Structure of human cyclin-dependent kinase inhibitor p19(INK4d): Comparison to known ankyrin-repeat-containing structures and implications for the dysfunction of tumor suppressor p16(INK4a)

Author keywords

CDK4 inhibitor; Cell cycle; p19(INK4d) p16(INK4a); Structure

Indexed keywords


EID: 0032532157     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00128-2     Document Type: Article
Times cited : (51)

References (42)
  • 1
    • 0029849620 scopus 로고    scopus 로고
    • Cancer cell cycles
    • Sherr, C.J. (1996). Cancer cell cycles. Science 274, 1672-1677.
    • (1996) Science , vol.274 , pp. 1672-1677
    • Sherr, C.J.1
  • 2
    • 0027938209 scopus 로고
    • Cyclins and cancer II: Cyclin D and CDK inhibitors come of age
    • Hunter, T. & Pines, J. (1994). Cyclins and cancer II: cyclin D and CDK inhibitors come of age. Cell 79, 573-582.
    • (1994) Cell , vol.79 , pp. 573-582
    • Hunter, T.1    Pines, J.2
  • 4
    • 0027769876 scopus 로고
    • A new regulatory motif in cell-cycle control causing specific inhibition of cyclin D/CDK4
    • Serrano, M., Hannon, G.J. & Beach, D. (1993). A new regulatory motif in cell-cycle control causing specific inhibition of cyclin D/CDK4. Nature 366, 704-707.
    • (1993) Nature , vol.366 , pp. 704-707
    • Serrano, M.1    Hannon, G.J.2    Beach, D.3
  • 5
    • 0028121279 scopus 로고
    • A cell cycle regulator potentially involved in genesis of many tumor types
    • Kamb, A., et al., & Skolnick, M.H. (1994). A cell cycle regulator potentially involved in genesis of many tumor types. Science 264, 436-440.
    • (1994) Science , vol.264 , pp. 436-440
    • Kamb, A.1    Skolnick, M.H.2
  • 6
    • 0030612469 scopus 로고    scopus 로고
    • The p19(INK4d) cyclin dependent kinase gene is altered in osteosarcoma
    • Miller, C.W., Yeon, C., Aslo, A., Mendoza, S., Aytac, U. & Koeffler, H.P. (1997). The p19(INK4d) cyclin dependent kinase gene is altered in osteosarcoma. Oncogene 15, 231-235.
    • (1997) Oncogene , vol.15 , pp. 231-235
    • Miller, C.W.1    Yeon, C.2    Aslo, A.3    Mendoza, S.4    Aytac, U.5    Koeffler, H.P.6
  • 7
    • 0028918388 scopus 로고
    • Novel INK4 proteins, p19 and p 18, are specific inhibitors of the cyclin D-dependent kinases CDK4 and CDK6
    • Hirai, H., et al, & Sherr, C.J. (1995). Novel INK4 proteins, p19 and p 18, are specific inhibitors of the cyclin D-dependent kinases CDK4 and CDK6. Mol. Cell Biol. 15, 2672-2682.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 2672-2682
    • Hirai, H.1    Sherr, C.J.2
  • 8
    • 8044223425 scopus 로고    scopus 로고
    • INK4/MTS1, p18 and p19 in human cancer cell lines
    • INK4/MTS1, p18 and p19 in human cancer cell lines. Int. J. Cancer 68, 605-611.
    • (1996) Int. J. Cancer , vol.68 , pp. 605-611
    • Gemma, A.1    Harris, G.G.2
  • 9
    • 0027333330 scopus 로고
    • Hundreds of ankyrin-like repeats in functionally diverse proteins: Mobile modules that cross phyla horizontally?
    • Bork, P. (1993). Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally? Proteins 17, 363-374.
    • (1993) Proteins , vol.17 , pp. 363-374
    • Bork, P.1
  • 11
    • 0029671263 scopus 로고    scopus 로고
    • INKd, a p16-related inhibitor specific to CDK6 and CDK4
    • INKd, a p16-related inhibitor specific to CDK6 and CDK4. Mol. Biol. Cell 7, 57-70.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 57-70
    • Guan, K.-L.1    Xiong, Y.2
  • 14
    • 0031991891 scopus 로고    scopus 로고
    • INK4a: Determination of solution structure and analyses of its interaction with cyclin-dependent kinase 4
    • INK4a: determination of solution structure and analyses of its interaction with cyclin-dependent kinase 4. Mol. Cell 1, 421-431.
    • (1998) Mol. Cell , vol.1 , pp. 421-431
    • Byeon, L.-J.1    Tsai, M.-D.2
  • 16
    • 0031007986 scopus 로고    scopus 로고
    • A consensus residue analysis of loop and helix-capping residues in four-α-helical-bundle proteins
    • Parker, M.H. & Hefford, M.A. (1997). A consensus residue analysis of loop and helix-capping residues in four-α-helical-bundle proteins. Protein Eng. 10, 487-496.
    • (1997) Protein Eng. , vol.10 , pp. 487-496
    • Parker, M.H.1    Hefford, M.A.2
  • 18
    • 0030623419 scopus 로고    scopus 로고
    • Role of a nonnative interaction in the folding of the protein G B1 domain as inferred from conformational analysis of the α-helix fragment
    • Blanco, F.J., Ortiz, A.R. & Serrano, L. (1997). Role of a nonnative interaction in the folding of the protein G B1 domain as inferred from conformational analysis of the α-helix fragment. Fold. Des. 2, 123-133.
    • (1997) Fold. Des. , vol.2 , pp. 123-133
    • Blanco, F.J.1    Ortiz, A.R.2    Serrano, L.3
  • 19
    • 0029665942 scopus 로고    scopus 로고
    • INK4a: Structural characterization of wild-type and mutant proteins by NMR and circular dichroism
    • INK4a: structural characterization of wild-type and mutant proteins by NMR and circular dichroism. Biochemistry 35, 9475-9487.
    • (1996) Biochemistry , vol.35 , pp. 9475-9487
    • Tevelev, A.1    Tsai, M.D.2
  • 20
    • 0032524455 scopus 로고    scopus 로고
    • The structural basis of ankyrin-like repeat function as revealed by the solution structure of myotrophin
    • Yang, Y., Sambasivarao, N., Sen, S. & Qin, J. (1998). The structural basis of ankyrin-like repeat function as revealed by the solution structure of myotrophin. Structure 6, 619-626.
    • (1998) Structure , vol.6 , pp. 619-626
    • Yang, Y.1    Sambasivarao, N.2    Sen, S.3    Qin, J.4
  • 21
    • 0030575866 scopus 로고    scopus 로고
    • Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of p53BP2
    • Svetlana, G. & Pavletich, N.P. (1996). Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of p53BP2. Science 274, 1001-1005.
    • (1996) Science , vol.274 , pp. 1001-1005
    • Svetlana, G.1    Pavletich, N.P.2
  • 22
    • 0032512459 scopus 로고    scopus 로고
    • The structure of GABPα/β: An ETS domainankyrin repeat heterodimer bound to DNA
    • Batchelor, A.H., Piper, D.E., de la Brousse, F.C., McKnight, S.L. & Wolberger, C. (1998). The structure of GABPα/β: an ETS domainankyrin repeat heterodimer bound to DNA. Science 279, 1037-1041.
    • (1998) Science , vol.279 , pp. 1037-1041
    • Batchelor, A.H.1    Piper, D.E.2    De La Brousse, F.C.3    McKnight, S.L.4    Wolberger, C.5
  • 24
    • 0032485025 scopus 로고    scopus 로고
    • Characterization of the cyclin-dependent kinase inhibitory domain of the INK4 family as a model for a synthetic tumor suppressor molecule
    • Fahraeus, R., Lain, S., Ball, K.L & Lane, D.P. (1998). Characterization of the cyclin-dependent kinase inhibitory domain of the INK4 family as a model for a synthetic tumor suppressor molecule. Oncogene 16, 587-596.
    • (1998) Oncogene , vol.16 , pp. 587-596
    • Fahraeus, R.1    Lain, S.2    Ball, K.L.3    Lane, D.P.4
  • 25
    • 0029980941 scopus 로고    scopus 로고
    • CDKN2 associated with familial melanoma
    • CDKN2 associated with familial melanoma. Mol. Cell Biol. 16, 3844-3852.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 3844-3852
    • Parry, D.1    Peters, G.2
  • 27
    • 0029802930 scopus 로고    scopus 로고
    • INK4 proteins encoded by tumor-derived alleles
    • INK4 proteins encoded by tumor-derived alleles.J. Biol. Chem. 271, 28734-28737.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28734-28737
    • Zhang, B.1    Peng, Z.2
  • 28
    • 0028971677 scopus 로고
    • p16 proteins from melanoma-prone families are deficient in binding to CDK6
    • Reymond, A. & Brent, R. (1995). p16 proteins from melanoma-prone families are deficient in binding to CDK6. Oncogene 11, 1173-1178.
    • (1995) Oncogene , vol.11 , pp. 1173-1178
    • Reymond, A.1    Brent, R.2
  • 33
    • 0003604443 scopus 로고
    • Isomorphous Replacement and Anomalous Scattering
    • SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1991). Isomorphous Replacement and Anomalous Scattering, Proceedings of the Daresbury Study Weekend. SERC Daresbury Laboratory, Warrington, UK.
    • (1991) Proceedings of the Daresbury Study Weekend
    • Otwinowski, Z.1
  • 34
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computing Project No. 4. (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 38
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum likelihood method
    • Murshudov, G.N., Vagin, A.A. & Dodson, E.J. (1997). Refinement of macromolecular structures by the maximum likelihood method. Acta Cryst. D 53, 240-255.
    • (1997) Acta Cryst. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 39
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Cryst. A 50, 157-163.
    • (1994) Acta Cryst. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 40
    • 0026607234 scopus 로고
    • The ANK repeat: A ubiquitous motif involved in macromolecular recognition
    • Michaely, P. & Bennett, V. (1992). The ANK repeat: a ubiquitous motif involved in macromolecular recognition. Trends Cell Biol. 2, 127-130.
    • (1992) Trends Cell Biol. , vol.2 , pp. 127-130
    • Michaely, P.1    Bennett, V.2
  • 42
    • 0000732609 scopus 로고
    • GRASP - Graphical representation and analysis of surface properties
    • Nicholls, A., Bharadwaj, R. & Honig, B. (1993). GRASP - graphical representation and analysis of surface properties. Biophys. J. 64, 166-169.
    • (1993) Biophys. J. , vol.64 , pp. 166-169
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.