PDBsum entry: 1apj

Extracellular matrix

PDB id: 1apj

Contents

Protein chain

74 a.a. *

* Residue conservation analysis

PDB id:

1apj

Name:

Extracellular matrix

Title:

Nmr study of the transforming growth factor beta binding protein-like domain (tb module/8-cys domain), nmr, 21 structures

Structure:

Fibrillin. Chain: a. Fragment: transforming growth factor beta binding protein- like domain 6(tb6), residues 2054 - 2125. Engineered: yes

Source:

Fragment: transforming growth factor beta binding protein- like domain 6(tb6), residues 2054-2125. Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

21 models

Authors:

X.Yuan,A.K.Downing,V.Knott,P.A.Handford

Key ref:

X.Yuan et al. (1997). Solution structure of the transforming growth factor beta-binding protein-like module, a domain associated with matrix fibrils. EMBO J, 16, 6659-6666. PubMed id: 9362480 DOI: 10.1093/emboj/16.22.6659

Date:

22-Jul-97 Release date: 28-Jan-98

Protein chain

P35555  (FBN1_HUMAN) -  Fibrillin-1

Seq: 2871 a.a.

Struc: 74 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 

• Biochemical function: binding (1 term)

DOI no: 10.1093/emboj/16.22.6659

EMBO J 16:6659-6666 (1997)

PubMed id: 9362480

Solution structure of the transforming growth factor beta-binding protein-like module, a domain associated with matrix fibrils.

X.Yuan, A.K.Downing, V.Knott, P.A.Handford.

ABSTRACT

Here we describe the high resolution nuclear magnetic resonance (NMR) structure of a transforming growth factor beta (TGF-beta)-binding protein-like (TB) domain, which comes from human fibrillin-1, the protein defective in the Marfan syndrome (MFS). This domain is found in fibrillins and latent TGF-beta-binding proteins (LTBPs) which are localized to fibrillar structures in the extracellular matrix. The TB domain manifests a novel fold which is globular and comprises six antiparallel beta-strands and two alpha-helices. An unusual cysteine triplet conserved in the sequences of TB domains is localized to the hydrophobic core, at the C-terminus of an alpha-helix. The structure is stabilized by four disulfide bonds which pair in a 1-3, 2-6, 4-7, 5-8 pattern, two of which are solvent exposed. Analyses of MFS-causing mutations and the fibrillin-1 cell-binding RGD site provide the first clues to the surface specificity of TB domain interactions. Modelling of a homologous TB domain from LTBP-1 (residues 1018-1080) suggests that hydrophobic contacts may play a role in its interaction with the TGF-beta1 latency-associated peptide.

Selected figure(s)

Figure 4.
Figure 4 Domain organization of proteins containing the TB domain consensus pattern of eight cysteine residues (see text).

Figure 5.
Figure 5 Comparison of the molecular surfaces of (A) fibrillin-1 TB6 and (B) TB domain (residues 1018 -1080) from LTBP-1. Hydrophobic residues (Ala, Leu, Val, Ile, Met, Pro, Phe, Tyr, Trp) are shown in red. The seventh cysteine in each domain is shaded in yellow. Cys1062 is adjacent to the FP insertion in the TB domain from LTBP-1.

The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (1997, 16, 6659-6666) copyright 1997.

Figures were selected by an automated process.