Structure of the BIR domain from ML-IAP bound to a peptidomimetic

Orally bioavailable antagonists of inhibitor of apoptosis proteins based on an azabicyclooctane scaffold

Design, synthesis, and biological activity of a potent Smac mimetic that sensitizes cancer cells to apoptosis by antagonizing IAPs.

Engineering ML-IAP to produce an extraordinarily potent caspase-9 inhibitor: implications for Smac-dependent anti-apoptotic activity of ML-IAP.

Structure and function analysis of peptide antagonists of melanoma inhibitor of apoptosis (ML-IAP)

Vertical focusing mirror; single crystal (Si111) bent monochromator (horizontal focusing).

Baculoviral IAP repeat-containing protein 7

Kidney inhibitor of apoptosis protein, KIAP, Melanoma inhibitor of apoptosis protein, ML-IAP, Livin, RING finger protein 50

MGSSHHHHHHSSGEVPRGSHMLETEEEEEEGAGATLSRGPAFPGMGSEELRLASFYDWPLTAEVPPELLAAAGFFHTGHQ
DKVRCFFCYGGLQSWKRGDDPWTEHAKWFPSCQFLLRSKGRDFVHSVQETHSQLLGSWDP

also known as KIAP OR MLIAP OR LIVIN, BIRC7, KIAP, LIVIN, MLIAP, RNF50, UNQ5800/PRO19607/PRO21344

SODIUM ACETATE, PEG 300, DTT, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

Authors state that each asymmetric unit contains five biological units, each containing one molecule of ML-IAP with either a peptide or a peptidomimetic bound at the active site. Chains A-D form a (not biologically relevant) tetramer in which molecule A binds a peptide consisting of part of the N-terminal unstructured region of molecule D; molecule B similarly binds part of molecule C; molecule C binds molecule B; and molecule D binds molecule A. The biologically relevant complex is formed by ML-IAP molecule E binding the peptidomimetic (ligand 389).

ZINC BINDING, PEPTIDE COMPLEX, APOPTOSIS INHIBITION, PEPTIDOMIMETIC, SMALL MOLECULE, DRUG DESIGN, Apoptosis, Metal-binding, Nucleus, Zinc-finger

TEEEEEEGAGATLSRGPAFPGMGSEELRLASFYDWPLTAEVPPELLAAAGFFHTGHQDKVRCFFCYGGLQSWKRGDDPWT
EHAKWFPSCQFLLRSKGRDFVHSVQETHSQLLGSWDP