We used molecular dynamics simulation to evaluate the association properties of C-terminal sterile a-motif (SAM) domain of human p73a. To test the dimerization propensity of this structure we carried out four simulations: EphB2 X-ray dimer, p73 modeled dimer, p73 NMR monomer, and p73 modeled monomer with an elongated helix 5. The results show a direct interaction between helix 5 and helix 3 since a conformational collapse of helix 3 is observed when dimer contact and/or an elongation of helix 5 is introduced by modeling in p73 SAM domain. On the basis of these results we suggest that the recognition properties of the SAM domains may be modulated by the conformational state of helix 5.
Falconi, M., Melino, G., Desideri, A. (2004). Molecular Dynamics Simulation of the C-terminal sterile alpha-motif (SAM) domain of human p73 alpha: evidence of a dynamical relationship between helices 3 and 5. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 316(4), 1037-1042 [10.1016/j.bbrc.2004.02.146].
Molecular Dynamics Simulation of the C-terminal sterile alpha-motif (SAM) domain of human p73 alpha: evidence of a dynamical relationship between helices 3 and 5.
FALCONI, MATTIA;MELINO, GENNARO;DESIDERI, ALESSANDRO
2004-01-01
Abstract
We used molecular dynamics simulation to evaluate the association properties of C-terminal sterile a-motif (SAM) domain of human p73a. To test the dimerization propensity of this structure we carried out four simulations: EphB2 X-ray dimer, p73 modeled dimer, p73 NMR monomer, and p73 modeled monomer with an elongated helix 5. The results show a direct interaction between helix 5 and helix 3 since a conformational collapse of helix 3 is observed when dimer contact and/or an elongation of helix 5 is introduced by modeling in p73 SAM domain. On the basis of these results we suggest that the recognition properties of the SAM domains may be modulated by the conformational state of helix 5.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
