PDBsum entry: 1jh5

Immune system, antitumor protein

PDB id: 1jh5

Contents

Protein chains

(+ 4 more) 144 a.a. *

* Residue conservation analysis

PDB id:

1jh5

Name:

Immune system, antitumor protein

Title:

Crystal structure of stall-1 of tnf family ligand

Structure:

Tumor necrosis factor ligand superfamily member 1 chain: a, b, c, d, e, f, g, h, i, j. Fragment: stall-1, soluble part of tall-1. Synonym: tnf family ligand. Tnf-and apol-related leukocyte ligand 1. Tall-1. B lymphocyte stimulator. Blys. B cell-act factor. Tumor necrosis factor (ligand) superfamily, member engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

60mer (from PQS)

Resolution:

3.00Å R-factor: 0.236 R-free: 0.252

Authors:

Y.Liu,L.Xu,N.Opalka,H.-B.Shu,G.Zhang

Key ref:

Y.Liu et al. (2002). Crystal structure of sTALL-1 reveals a virus-like assembly of TNF family ligands. Cell, 108, 383-394. PubMed id: 11853672 DOI: 10.1016/S0092-8674(02)00631-1

Date:

27-Jun-01 Release date: 08-Feb-02

Protein chains

Q9Y275  (TN13B_HUMAN) -  Tumor necrosis factor ligand superfamily member 13B

Seq: 285 a.a.

Struc: 144 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: membrane (1 term)
• Biological process: immune response (1 term)
• Biochemical function: protein binding (2 terms)

DOI no: 10.1016/S0092-8674(02)00631-1

Cell 108:383-394 (2002)

PubMed id: 11853672

Crystal structure of sTALL-1 reveals a virus-like assembly of TNF family ligands.

Y.Liu, L.Xu, N.Opalka, J.Kappler, H.B.Shu, G.Zhang.

ABSTRACT

TALL-1/BAFF/BLyS was recently identified as a member of the tumor necrosis factor (TNF) ligand family. The crystal structure of the functional soluble TALL-1 (sTALL-1) has been determined at 3.0 A. sTALL-1 forms a virus-like assembly with 200 A diameter in the crystals, containing 60 sTALL-1 monomers. The cluster formation is mediated by a "flap" region of the sTALL-1 monomer. The virus-like assembly was also detected in solution using gel filtration and electron microscopy. Deletion of the flap region disrupted the formation of the virus-like assembly. The mutant sTALL-1 still bound its receptor but could not activate NF-kappaB and did not stimulate B lymphocyte proliferation. Finally, we found the virus-like cluster of sTALL-1 exists in physiological condition. We propose that this virus-like assembly of sTALL-1 is the functional unit for TALL-1 in vivo.

Selected figure(s)

Figure 2.
Figure 2. The Relative Position of an Asymmetry Unit in the Cluster and Overall Structures of the Cluster at Different Orientations(A) The ten monomers (yellow) in the asymmetric unit, which generate the left 50 monomers (colored gray) through crystallographic symmetry (P6[3]22) to form the virus-like cluster with total of 60 monomers.(B) The structure of virus-like cluster (T = 1) looking down from the local five-fold symmetry, and (C) looking down from the three-fold symmetry. All monomers are colored according to chains as default set in RIBBON (Carson, 1987).

Figure 7.
Figure 7. Structure-Based Sequence Alignments of TNF Ligand Family Members at the Region Spanning β Strands D and EConserved hydrophobic residues are bold. Sequence source is from Locksley et al., 2001.

The above figures are reprinted by permission from Cell Press: Cell (2002, 108, 383-394) copyright 2002.

Figures were selected by an automated process.