Literature summary for 2.7.7.31 extracted from

Loch, J.; Rosario, S.; Delarue, M.
Structural basis for a new templated activity by terminal deoxynucleotidyl transferase: implications for V(D)J recombination (2016), Structure, 24, 1452-1463.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
TdT in complex with dsDNA A5/T5G and ddCTP, to 2.80 A resolution, TdT in complex with dsDNA A5/T5GG and ddCTP to 1.99 A resolution and TdT in complex with ssDNA A5, dsDNA A5/T5GG-P, and ddCTP to 2.66 A resolution	Mus musculus

Protein Variants

Protein Variants	Comment	Organism
D179A	mutation improves templated-polymerase activity	Mus musculus
S187R	mutation improves templated-polymerase activity	Mus musculus
S187R/D179A	mutation improves templated-polymerase activity	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	P09838	-	-

General Information

General Information	Comment	Organism
physiological function	TdT also has a templated-polymerase activity, in the presence of higher concentrations of a downstream DNA duplex, and performs a micro-homology single base-pair search to align the DNA synapsis. Both templated and untemplated activities of TdT are needed to explain the distributions of lengths of N regions observed experimentally in T cell receptors and antibodies	Mus musculus

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Release 2023.1 (January 2023)