1apj

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[[Image:1apj.gif|left|200px]]
[[Image:1apj.gif|left|200px]]
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{{Structure
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{{STRUCTURE_1apj| PDB=1apj | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1apj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apj OCA], [http://www.ebi.ac.uk/pdbsum/1apj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1apj RCSB]</span>
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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.]]
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[[Category: connective tissue]]
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[[Category: Connective tissue]]
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[[Category: extracellular matrix]]
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[[Category: Extracellular matrix]]
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[[Category: fibrillin fragment]]
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[[Category: Fibrillin fragment]]
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[[Category: marfan syndrome]]
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[[Category: Marfan syndrome]]
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[[Category: microfibril]]
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[[Category: Microfibril]]
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[[Category: novel fold]]
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[[Category: Novel fold]]
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[[Category: tb module]]
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[[Category: Tb module]]
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Revision as of 07:33, 2 May 2008

Template:STRUCTURE 1apj

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

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