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PDBsum entry 3m1d
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Metal binding protein
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PDB id
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3m1d
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Metal binding protein
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Title:
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Structure of bir1 from ciap1
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Structure:
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Baculoviral iap repeat-containing protein 2. Chain: a, b. Fragment: bir1. Synonym: inhibitor of apoptosis protein 2, iap-2, hiap-2, hiap2, c- iap1, tnfr2-traf-signaling complex protein 2, iap homolog b, ring finger protein 48. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.00Å
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R-factor:
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0.198
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R-free:
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0.232
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Authors:
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P.D.Mace,C.L.Day
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Key ref:
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P.D.Mace
et al.
(2010).
Asymmetric recruitment of cIAPs by TRAF2.
J Mol Biol,
400,
8.
PubMed id:
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Date:
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04-Mar-10
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Release date:
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26-May-10
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PROCHECK
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Headers
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References
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Q13490
(BIRC2_HUMAN) -
Baculoviral IAP repeat-containing protein 2 from Homo sapiens
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Seq:
Struc:
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618 a.a.
78 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.2.3.2.27
- RING-type E3 ubiquitin transferase.
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Reaction:
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6- ubiquitinyl-[acceptor protein]-L-lysine
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J Mol Biol
400:8
(2010)
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PubMed id:
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Asymmetric recruitment of cIAPs by TRAF2.
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P.D.Mace,
C.Smits,
D.L.Vaux,
J.Silke,
C.L.Day.
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ABSTRACT
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Cellular inhibitor of apoptosis protein (cIAP) 1 and cIAP2 set the balance
between transcription factor and apoptosis signaling downstream of tumor
necrosis factor (TNF) receptor superfamily members by acting as ubiquitin E3
ligases for substrates that are part of the TNF receptor complex. To fulfill
this role, cIAPs must be recruited to the receptor complex by
TNF-receptor-associated factor (TRAF) 2. In this study, we reconstituted the
complex between baculoviral IAP repeat (BIR) 1 of cIAP1 and the coiled-coil
region of TRAF2, solved the structure of BIR1 from cIAP1, and mapped key binding
residues on each molecule using mutagenesis. Biophysical analysis indicates that
a single BIR1 domain binds the trimeric TRAF2 coiled-coil domain. This suggests
that only one IAP molecule binds to each TRAF trimer and makes it likely that
the dimeric cIAPs crosslink two TRAF trimers.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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C.Zheng,
Q.Yin,
and
H.Wu
(2011).
Structural studies of NF-κB signaling.
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Cell Res,
21,
183-195.
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H.Häcker,
P.H.Tseng,
and
M.Karin
(2011).
Expanding TRAF function: TRAF3 as a tri-faced immune regulator.
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Nat Rev Immunol,
11,
457-468.
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J.Lopez,
and
P.Meier
(2010).
To fight or die - inhibitor of apoptosis proteins at the crossroad of innate immunity and death.
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Curr Opin Cell Biol,
22,
872-881.
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M.Gyrd-Hansen,
and
P.Meier
(2010).
IAPs: from caspase inhibitors to modulators of NF-kappaB, inflammation and cancer.
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Nat Rev Cancer,
10,
561-574.
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P.D.Mace,
and
S.J.Riedl
(2010).
Molecular cell death platforms and assemblies.
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Curr Opin Cell Biol,
22,
828-836.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
