1apj
From Proteopedia
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NMR STUDY OF THE TRANSFORMING GROWTH FACTOR BETA BINDING PROTEIN-LIKE DOMAIN (TB MODULE/8-CYS DOMAIN), NMR, 21 STRUCTURES
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Aortic aneurysm, ascending, and dissection OMIM:[134797], Ectopia lentis, familial OMIM:[134797], MASS syndrome OMIM:[134797], Marfan syndrome OMIM:[134797], Shprintzen-Goldberg syndrome OMIM:[134797], Weill-Marchesani syndrome, dominant OMIM:[134797]
About this Structure
1APJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the transforming growth factor beta-binding protein-like module, a domain associated with matrix fibrils., Yuan X, Downing AK, Knott V, Handford PA, EMBO J. 1997 Nov 17;16(22):6659-66. PMID:9362480
Page seeded by OCA on Mon Nov 12 16:00:56 2007
