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'''NMR STUDY OF THE TRANSFORMING GROWTH FACTOR BETA BINDING PROTEIN-LIKE DOMAIN (TB MODULE/8-CYS DOMAIN), NMR, 21 STRUCTURES''' | '''NMR STUDY OF THE TRANSFORMING GROWTH FACTOR BETA BINDING PROTEIN-LIKE DOMAIN (TB MODULE/8-CYS DOMAIN), NMR, 21 STRUCTURES''' | ||
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[[Category: Knott, V.]] | [[Category: Knott, V.]] | ||
[[Category: Yuan, X.]] | [[Category: Yuan, X.]] | ||
[[Category: | [[Category: Connective tissue]] | ||
[[Category: | [[Category: Extracellular matrix]] | ||
[[Category: | [[Category: Fibrillin fragment]] | ||
[[Category: | [[Category: Marfan syndrome]] | ||
[[Category: | [[Category: Microfibril]] | ||
[[Category: | [[Category: Novel fold]] | ||
[[Category: | [[Category: Tb module]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:33:17 2008'' | |||
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Revision as of 07:33, 2 May 2008
NMR STUDY OF THE TRANSFORMING GROWTH FACTOR BETA BINDING PROTEIN-LIKE DOMAIN (TB MODULE/8-CYS DOMAIN), NMR, 21 STRUCTURES
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.
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 Fri May 2 10:33:17 2008
