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c-IAP1 and c-IAP2: inhibitors of apoptosis
| Details |
Inventors: Rothe, Mike; Goeddel, David V.;
Assignee: Tularik Inc. (South San Francisco, CA)
Primary Examiner: Hauda; Karen M.
Assistant Examiner: Woitach; Joseph T.
Attorney, Agent or Firm: Osman; Richard Aron
The invention provides methods and compositions relating to novel human cellular inhibitor of apoptosis proteins (c-IAP1/2) comprising a series of defined structural domain repeats and/or a RING finger domain; in particular, at least two of: a particular first domain repeat, a particular second domain repeat, and a particular third domain repeat, and/or a particular RING finger domain. The proteins provide a c-IAP specific function, with preferred proteins being capable of modulating the induction of apoptosis; for example, by binding a human tumor necrosis factor receptor associated factor (TRAF). The compositions include nucleic acids which encode the subject c-IAP and hybridization probes and primers capable of hybridizing with the disclosed c-IAP genes. |
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DETAILED DESCRIPTION OF THE INVENTION The invention provides methods and compositions relating to novel cellular inhibitor of apoptosis proteins (c-IAPs).
The nucleotide sequence of a natural cDNA encoding human c-IAP is shown as SEQUENCE ID NO: 1 and the full conceptual translate is shown as SEQUENCE ID NO:2.
The nucleotide sequence of another natural cDNA encoding human c-IAP2 is shown as SEQUENCE ID NO:3 and the full conceptual translate is shown as SEQUENCE ID NO:4.
The human c-IAPs of the invention include incomplete translates of SEQUENCE ID NOS:1 and 3 or deletions mutants of SEQUENCE ID NOS: 2 and/or 4, which translates or deletions mutants have at least one of the human c-LAP specific activities described herein.
In addition, the invention provides nonhuman mammalian homologs of the disclosed human c-IAPs.
These homologs are encoded by natural cDNAs which are capable of specifically hybridizing with one or more of the disclosed human cDNAs under hybridization conditions describe below and are isolated using the methods and reagents described herein.
For example, the amino acid sequence of a murine homolog of c-IAP1, and the sequence its cDNA are shown in SEQUENCE ID NOS: 14 and 13.
The subject proteins comprise a series of defined structural domain repeats and/or a RING fmger domain shown to be necessary for human c-IAP specific function; generally including at least two of: a first domain repeat comprising SEQUENCE ID NO: 5, 6 or a consensus of 5 and 6, a second domain repeat comprising SEQUENCE ID NO: 7, 8 or a consensus of 7 and 8, and a third domain repeat comprising SEQUENCE ID NO: 9, 10 or a consensus of 9 and 10; and/or a RING finger domain comprising SEQUENCE ID NO: 11, 12 or a consensus of 11 and 12.
Preferred domain repeat containing c-IAPs contain each of the three domain repeats.
More preferred c-IAPs comprise the three domain repeats and the C-terminal RING finger.
To secure or optimize the requisite function for the protein, the repeats are usually preceded (N-terminally) and separated by intervening regions of about 10 to about 100 residues, which regions preferably derive from those found in the natural c-IAP1 and c-IAP2 translates
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Gene Therapy 
