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A stereo view of the superposition of the 20 lowest energy NMR structures of the N-terminal domain of the human T-cell leukemia virus type 1 (HTLV-1) Capsid protein. Helices are color coded. |
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Comparison of the N-terminal Capsid Protein of HIV-1 (green) and HTLV-1 (yellow). |
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Detail comparison of the AGPL/I motif in Capsid proteins. This motif is important for Cyclophilin A (Cyp A) binding to Hiv-1 Capsid. Cyp A does not bind HTLV-1 Capsid. The structural comparison shows that the HIV-1 P90 cis-trans isomerization and greater loop exposure facilitates Cyp A interaction. |
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Asp-Pro salt bridge stabilizes the orientation of the β-hairpin in the Capsid protein. A small difference in the salt bridge conformation leads to the overall change in the β-hairpin orientation. |
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Comparison of NMR structures of Bcl-2 family of proteins shows great similarity while their functions are exactly opposite. |
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Structural comparison of Bax and Bcl-xL + BH3 peptide reveals similar fold. The molecular interaction stabilizing the BH3 peptide in the hydrophobic pocket of Bcl-xL is also quite similar to the ones stabilizing helix a9 in Bax. Note the reverse orientation of the BH3 peptide in Bcl-xL hydrophobic pocket relative to the a9 helix in Bax. |
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Comparison of the N-terminal tail of the human and yeast Fis1 protein. The yeast Fis1 N-terminal sits in the hydrophobic groove of the protein. The hydrophobic interaction between the N-terminal tail and the groove is complemented by electrostatic interactions at the its perimeter. Truncation of this N-terminal tail abolishes Mdv1 recruitment to the mitochondria membrane, thus inhibiting mitochondria fission. This is illustrated by the diffuse profile of the GFP-Mdv1 confocal in yeast transfected with N-terminal truncated Fis1. |
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