1vyb: Difference between revisions

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==Overview==
==Overview==
The human L1 endonuclease (L1-EN) is encoded by the non-LTR, retrotransposon LINE-1 (L1). L1 is responsible for more than 1.5 million, retrotransposition events in the history of the human genome, contributing, more than a quarter to human genomic DNA (L1 and Alu elements). L1-EN is, related to the well-understood human DNA repair endonuclease APE1, and its, nicking specificity is a major determinant for retrotransposon integration, site selection. The crystal structure of human L1 endonuclease is the, first of a retrotransposon-encoded protein and a prototype for, retrotransposon-encoded endonucleases involved in target-primed reverse, transcription. Structure-based endonuclease alignments reveal a conserved, threonine in addition to previously identified invariant residues and, suggest that DNA recognition proceeds via the accommodation of an, extrahelical nucleotide within a pocket of the enzyme. The present, analysis will help to refine phylogenetic and functional relationships, among metal-dependent phosphohydrolases and provides a basis for, manipulating non-LTR retrotransposon integration site selection.
The human L1 endonuclease (L1-EN) is encoded by the non-LTR retrotransposon LINE-1 (L1). L1 is responsible for more than 1.5 million retrotransposition events in the history of the human genome, contributing more than a quarter to human genomic DNA (L1 and Alu elements). L1-EN is related to the well-understood human DNA repair endonuclease APE1, and its nicking specificity is a major determinant for retrotransposon integration site selection. The crystal structure of human L1 endonuclease is the first of a retrotransposon-encoded protein and a prototype for retrotransposon-encoded endonucleases involved in target-primed reverse transcription. Structure-based endonuclease alignments reveal a conserved threonine in addition to previously identified invariant residues and suggest that DNA recognition proceeds via the accommodation of an extrahelical nucleotide within a pocket of the enzyme. The present analysis will help to refine phylogenetic and functional relationships among metal-dependent phosphohydrolases and provides a basis for manipulating non-LTR retrotransposon integration site selection.


==About this Structure==
==About this Structure==
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[[Category: transferase]]
[[Category: transferase]]


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