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PDBsum entry 3d9t

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protein ligands metals Protein-protein interface(s) links
Apoptosis PDB id
3d9t
Jmol
Contents
Protein chains
90 a.a. *
95 a.a. *
Ligands
ALA-THR-PRO-PHE-
GLN
ALA-THR-PRO-PHE-
GLN-GLU
Metals
_ZN ×2
Waters ×268
* Residue conservation analysis
PDB id:
3d9t
Name: Apoptosis
Title: Ciap1-bir3 in complex with n-terminal peptide from caspase- 9 (atpfqe)
Structure: Baculoviral iap repeat-containing protein 2. Chain: a, b. Synonym: inhibitor of apoptosis protein 2, hiap2, hiap-2, c-iap1, tnfr2-traf-signaling complex protein 2, iap homolog b, ring finger protein 48. Engineered: yes. Caspase-9. Chain: c, d. Synonym: casp-9, ice-like apoptotic protease 6, ice-lap6,
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: birc2, api1, iap2, mihb, rnf48. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: peptide synthesized based on n-terminal fragment of caspase-9 (atpfqe).
Resolution:
1.50Å     R-factor:   0.186     R-free:   0.205
Authors: R.Kulathila,A.Price
Key ref: R.Kulathila et al. (2009). The structure of the BIR3 domain of cIAP1 in complex with the N-terminal peptides of SMAC and caspase-9. Acta Crystallogr D Biol Crystallogr, 65, 58-66. PubMed id: 19153467 DOI: 10.1107/S0907444908039243
Date:
27-May-08     Release date:   10-Jun-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q13490  (BIRC2_HUMAN) -  Baculoviral IAP repeat-containing protein 2
Seq:
Struc:
 
Seq:
Struc:
618 a.a.
90 a.a.
Protein chain
Pfam   ArchSchema ?
Q13490  (BIRC2_HUMAN) -  Baculoviral IAP repeat-containing protein 2
Seq:
Struc:
 
Seq:
Struc:
618 a.a.
95 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 

 
DOI no: 10.1107/S0907444908039243 Acta Crystallogr D Biol Crystallogr 65:58-66 (2009)
PubMed id: 19153467  
 
 
The structure of the BIR3 domain of cIAP1 in complex with the N-terminal peptides of SMAC and caspase-9.
R.Kulathila, B.Vash, D.Sage, S.Cornell-Kennon, K.Wright, J.Koehn, T.Stams, K.Clark, A.Price.
 
  ABSTRACT  
 
The inhibitor of apoptosis protein (IAP) family of molecules inhibit apoptosis through the suppression of caspase activity. It is known that the XIAP protein regulates both caspase-3 and caspase-9 through direct protein-protein interactions. Specifically, the BIR3 domain of XIAP binds to caspase-9 via a ;hotspot' interaction in which the N-terminal residues of caspase-9 bind in a shallow groove on the surface of XIAP. This interaction is regulated via SMAC, the N-terminus of which binds in the same groove, thus displacing caspase-9. The mechanism of suppression of apoptosis by cIAP1 is less clear. The structure of the BIR3 domain of cIAP1 (cIAP1-BIR3) in complex with N-terminal peptides from both SMAC and caspase-9 has been determined. The binding constants of these peptides to cIAP1-BIR3 have also been determined using the surface plasmon resonance technique. The structures show that the peptides interact with cIAP1 in the same way that they interact with XIAP: both peptides bind in a similar shallow groove in the BIR3 surface, anchored at the N-terminus by a charge-stabilized hydrogen bond. The binding data show that the SMAC and caspase-9 peptides bind with comparable affinities (85 and 48 nM, respectively).