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Structure–activity based study of the Smac-binding pocket within the BIR3 domain of XIAP by Aislyn D. Wist; Lichuan Gu; Stefan J. Riedl; Yigong Shi; George L. McLendon is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Structure–activity based study of the Smac-binding pocket within the BIR3 domain of XIAP about?

A small series of peptide mimics was designed and synthesized to contain a heterocyclic ring in place of the potentially labile N-terminal peptide bond of the tetrapeptide containing the Smac-XIAP-binding motif. Two Smac mimics were shown to bind to the BIR3 domain of XIAP with moderate affinity and one displayed increased activity in cells relative to the Smac peptides. The structures of BIR3-XIAP in complex with a Smac peptide and a peptide mimic were solved and analyzed to elucidate the structure-activity relationship surrounding the Smac-binding domain within BIR3-XIAP.

Who reads Structure–activity based study of the Smac-binding pocket within the BIR3 domain of XIAP?

Author

Aislyn D. Wist; Lichuan Gu; Stefan J. Riedl; Yigong Shi; George L. McLendon

Publisher

Elsevier Science; Elsevier ; Elsevier Ltd.; Elsevier BV (ISSN 0968-0896)

Published

2007

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)