1APJ

NMR STUDY OF THE TRANSFORMING GROWTH FACTOR BETA BINDING PROTEIN-LIKE DOMAIN (TB MODULE/8-CYS DOMAIN), NMR, 21 STRUCTURES

Summary for 1APJ

• Entry DOI: 10.2210/pdb1apj/pdb
• Descriptor: FIBRILLIN (1 entity in total)
• Functional Keywords: fibrillin fragment, microfibril, tb module, marfan syndrome, connective tissue, novel fold, extracellular matrix
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 8018.97

Authors

Yuan, X.,Downing, A.K.,Knott, V.,Handford, P.A. (deposition date: 1997-07-22, release date: 1998-01-28, Last modification date: 2024-11-20)

Primary citation

Yuan, X.,Downing, A.K.,Knott, V.,Handford, P.A.
Solution structure of the transforming growth factor beta-binding protein-like module, a domain associated with matrix fibrils.
EMBO J., 16:6659-6666, 1997

PubMed 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.

PubMed: 9362480
DOI: 10.1093/emboj/16.22.6659

Experimental method

SOLUTION NMR