Title : Structure of human Rad51 protein filament from molecular modeling and site-specific linear dichroism spectroscopy.

Pub. Date : 2009 Aug 11

PMID : 19587234






3 Functional Relationships(s)
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1 We build our structure on reported structures for central and N-terminal parts of pure (uncomplexed) Rad51 protein by aid of linear dichroism spectroscopy, providing angular orientations of substituted tyrosine residues of Rad51-dsDNA filaments in solution. Tyrosine RAD51 recombinase Homo sapiens
2 We build our structure on reported structures for central and N-terminal parts of pure (uncomplexed) Rad51 protein by aid of linear dichroism spectroscopy, providing angular orientations of substituted tyrosine residues of Rad51-dsDNA filaments in solution. Tyrosine RAD51 recombinase Homo sapiens
3 The model suggests that the extension of a single-stranded DNA molecule upon binding of Rad51 is ensured by intercalation of Tyr-232 of the L1 loop, which might act as a docking tool, aligning protein monomers along the DNA strand upon filament assembly. Tyrosine RAD51 recombinase Homo sapiens