Structure of an ML-IAP/XIAP chimera 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)

Single crystal, cylindrically bent, Si(220)

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
DKVRCFFCYGGLQSWKRGDDPWTEHAKWFPGCQFLLRSKGQEYINNIHLTHSL

BIRC7, KIAP, LIVIN, MLIAP, RNF50, UNQ5800/PRO19607/PRO21344

LITHIUM SULFATE, PEG 3350, BIS-TRIS, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

1.3 A STRUCTURE OF THE ML-IAP/XIAP PROTEIN BOUND TO A DIFFERENT PEPTIDOMIMETIC, WITH THE LIGAND AND SURROUNDING WATERS REMOVED

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

Authors state that each asymmetric unit contains two biological assemblies of protein and ligand

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

TEEEEEEGAGATLSRGPAFPGMGSEELRLASFYDWPLTAEVPPELLAAAGFFHTGHQDKVRCFFCYGGLQSWKRGDDPWT
EHAKWFPSCQFLLRSKGRDFVHSVQETHSQLLGSWDP