Tubulin tyrosine ligase
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ContentsFunctionTubulin tyrosine ligase (TTL) adds tyrosine in an ATP-dependent reaction to the C-terminal of a detyrosinated a-tubulin. The detyrosination of α-tubulin is a posttranslational modification which exposes glutamate in the new tubulin C-terminal. The detyrosinated α-tubulin forms Glu-microtubules[1]. The complex of TTL and tubulin contains Stathmin (STM) - another tubulin-binding protein[2]. DiseaseMutated TTL causes morphogenic abnormalities and cancer. There is a loss of TTL activity during tumor growth[3]. Structural highlightsTubulin tyrosine ligase complex with α-tubulin (2 chains), β-tubulin (2 chains), and stathmin. TTL structure is composed of N-terminal, central and C-terminal domains. TTL interacts with α- and β-tubulin via 3 loops and one helix terminal[4]. 3D Structures of tubulin tyrosine ligaseTubulin tyrosine ligase 3D structures References
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This page was last modified 09:41, 5 February 2024.