Subcellular localization is an important feature of proteins which is closely correlated to their function. In this work,we tried to develop a new coding method of using those location predictive molecular function te...Subcellular localization is an important feature of proteins which is closely correlated to their function. In this work,we tried to develop a new coding method of using those location predictive molecular function terms of protein as the input for the prediction of subcellular localization. Combined with the amino acid pair composition of the sequence,this coding system is proved to be efficient for support vector machine (SVM) and to have satisfied performance when tested on the RH dataset. Meanwhile,the model also shows robustness against N-terminal uncertainties in sequences.展开更多
Bax, a pro-apoptotic member of the Bcl-2 family, changes intracellular location as it accelerates cell death. Bax consists of 9 α-helices where the assembly of helices α1-α8 resembles that of the anti-apoptotic pro...Bax, a pro-apoptotic member of the Bcl-2 family, changes intracellular location as it accelerates cell death. Bax consists of 9 α-helices where the assembly of helices α1-α8 resembles that of the anti-apoptotic protein, Bcl-xL. The opposite biological functions between Bcl-xL and Bax stem from relatively minor differences in their structures. The C-terminal α helix, that functions in mitochondrial membrane targeting, sits in the hydrophobic BH3 binding pocket proposed previously to mediate heterodimer formation among Bcl-2 family members. The structure of soluble Bax shows that the conformation of the C-terminal helix may simultaneously inhibit BH3 peptide binding associated with dimer formation and mitochondrial展开更多
TRAF2 is a critical adaptor molecule for TNF receptors in inflammatory and immune signaling. Upon receptor engagement, TRAF2 is recruited to CD40 and translocates to lipid rafts in a RING finger-dependent process, whi...TRAF2 is a critical adaptor molecule for TNF receptors in inflammatory and immune signaling. Upon receptor engagement, TRAF2 is recruited to CD40 and translocates to lipid rafts in a RING finger-dependent process, which enables the activation of downstream kinases. TRAF1 can displace TRAF2 and CD40 from raft fractions, and it promotes the ability of TRAF2 to sustain signal activation. Replacement of the RING finger of TRAF2 with a raft-targeting signal restores JNK activation and association with the cytoskeletal protein Filamin, but not NF-KB activation. TRAF1-/-dendritic cells show attenuated展开更多
文摘Subcellular localization is an important feature of proteins which is closely correlated to their function. In this work,we tried to develop a new coding method of using those location predictive molecular function terms of protein as the input for the prediction of subcellular localization. Combined with the amino acid pair composition of the sequence,this coding system is proved to be efficient for support vector machine (SVM) and to have satisfied performance when tested on the RH dataset. Meanwhile,the model also shows robustness against N-terminal uncertainties in sequences.
文摘Bax, a pro-apoptotic member of the Bcl-2 family, changes intracellular location as it accelerates cell death. Bax consists of 9 α-helices where the assembly of helices α1-α8 resembles that of the anti-apoptotic protein, Bcl-xL. The opposite biological functions between Bcl-xL and Bax stem from relatively minor differences in their structures. The C-terminal α helix, that functions in mitochondrial membrane targeting, sits in the hydrophobic BH3 binding pocket proposed previously to mediate heterodimer formation among Bcl-2 family members. The structure of soluble Bax shows that the conformation of the C-terminal helix may simultaneously inhibit BH3 peptide binding associated with dimer formation and mitochondrial
文摘TRAF2 is a critical adaptor molecule for TNF receptors in inflammatory and immune signaling. Upon receptor engagement, TRAF2 is recruited to CD40 and translocates to lipid rafts in a RING finger-dependent process, which enables the activation of downstream kinases. TRAF1 can displace TRAF2 and CD40 from raft fractions, and it promotes the ability of TRAF2 to sustain signal activation. Replacement of the RING finger of TRAF2 with a raft-targeting signal restores JNK activation and association with the cytoskeletal protein Filamin, but not NF-KB activation. TRAF1-/-dendritic cells show attenuated
