PDBsum entry: 2gkw

Apoptosis

PDB id: 2gkw

Contents

Protein chains

192 a.a. *

17 a.a. *

* Residue conservation analysis

PDB id:

2gkw

Name:

Apoptosis

Title:

Key contacts promote recongnito of baff-r by traf3

Structure:

Tnf receptor-associated factor 3. Chain: a. Fragment: traf domain. Synonym: cd40 receptor-associated factor 1, craf1, cd40-bin protein, cd40bp, lmp1-associated protein, lap1, cap-1. Engineered: yes. Tumor necrosis factor receptor superfamily member chain: b. Fragment: residues 160-183.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: traf3, cap1, craf1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Other_details: the sequence of this protein naturally exist sapiens (human).

Biol. unit:

Hexamer (from PDB file)

Resolution:

2.70Å R-factor: 0.220 R-free: 0.260

Authors:

K.R.Ely

Key ref:

C.Z.Ni et al. (2004). Key molecular contacts promote recognition of the BAFF receptor by TNF receptor-associated factor 3: implications for intracellular signaling regulation. J Immunol, 173, 7394-7400. PubMed id: 15585864 Ref: Full text

Date:

03-Apr-06 Release date: 11-Apr-06

Protein chain

Q13114  (TRAF3_HUMAN) -  TNF receptor-associated factor 3

Seq: 568 a.a.

Struc: 192 a.a.

Protein chain

No UniProt id for this chain

 Gene Ontology (GO) functional annotation 

• Biochemical function: protein binding (1 term)

Full text	J Immunol 173:7394-7400 (2004)
PubMed id: 15585864

Key molecular contacts promote recognition of the BAFF receptor by TNF receptor-associated factor 3: implications for intracellular signaling regulation.

C.Z.Ni, G.Oganesyan, K.Welsh, X.Zhu, J.C.Reed, A.C.Satterthwait, G.Cheng, K.R.Ely.

ABSTRACT

B cell-activating factor belonging to the TNF family receptor (BAFF-R), a member of the TNFR superfamily, plays a role in autoimmunity after ligation with BAFF ligand (also called TALL-1, BLyS, THANK, or zTNF4). BAFF/BAFF-R interactions are critical for B cell regulation, and signaling from this ligand-receptor complex results in NF-kappaB activation. Most TNFRs transmit signals intracellularly by recruitment of adaptor proteins called TNFR-associated factors (TRAFs). However, BAFF-R binds only one TRAF adaptor, TRAF3, and this interaction negatively regulates activation of NF-kappaB. In this study, we report the crystal structure of a 24-residue fragment of the cytoplasmic portion of BAFF-R bound in complex with TRAF3. The recognition motif (162)PVPAT(166) in BAFF-R is accommodated in the same binding crevice on TRAF3 that binds two related TNFRs, CD40 and LTbetaR, but is presented in a completely different structural framework. This region of BAFF-R assumes an open conformation with two extended strands opposed at right angles that each make contacts with TRAF3. The recognition motif is located in the N-terminal arm and intermolecular contacts mediate TRAF recognition. In the C-terminal arm, key stabilizing contacts are made, including critical hydrogen bonds with Gln(379) in TRAF3 that define the molecular basis for selective binding of BAFF-R solely to this member of the TRAF family. A dynamic conformational adjustment of Tyr(377) in TRAF3 occurs forming a new intermolecular contact with BAFF-R that stabilizes the complex. The structure of the complex provides a molecular explanation for binding affinities and selective protein interactions in TNFR-TRAF interactions.