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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/SESN2_HUMAN SESN2_HUMAN] Involved in the reduction of peroxiredoxins.<ref>PMID:15105503</ref> | | [https://www.uniprot.org/uniprot/SESN2_HUMAN SESN2_HUMAN] Involved in the reduction of peroxiredoxins.<ref>PMID:15105503</ref> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Eukaryotic cells coordinate growth with the availability of nutrients through mTOR complex 1 (mTORC1), a master growth regulator. Leucine is of particular importance and activates mTORC1 via the Rag GTPases and their regulators GATOR1 and GATOR2. Sestrin2 interacts with GATOR2 and is a leucine sensor. We present the 2.7-A crystal structure of Sestrin2 in complex with leucine. Leucine binds through a single pocket that coordinates its charged functional groups and confers specificity for the hydrophobic side chain. A loop encloses leucine and forms a lid-latch mechanism required for binding. A structure-guided mutation in Sestrin2 that decreases its affinity for leucine leads to a concomitant increase in the leucine concentration required for mTORC1 activation in cells. These results provide a structural mechanism of amino acid sensing by the mTORC1 pathway.
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| Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway.,Saxton RA, Knockenhauer KE, Wolfson RL, Chantranupong L, Pacold ME, Wang T, Schwartz TU, Sabatini DM Science. 2015 Nov 19. pii: aad2087. PMID:26586190<ref>PMID:26586190</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 5dj4" style="background-color:#fffaf0;"></div>
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| == References == | | == References == |
| <references/> | | <references/> |
