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1ksq

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{{STRUCTURE_1ksq| PDB=1ksq | SCENE= }}
{{STRUCTURE_1ksq| PDB=1ksq | SCENE= }}
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'''NMR Study of the Third TB Domain from Latent Transforming Growth Factor-beta Binding Protein-1'''
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===NMR Study of the Third TB Domain from Latent Transforming Growth Factor-beta Binding Protein-1===
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==Overview==
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Almost all TGF-beta is secreted as part of a large latent complex. This complex is formed from three molecules, a latent transforming growth factor-beta binding protein (LTBP), which plays roles in targeting and activation, a latency associated peptide (LAP), which regulates latency, and the TGF-beta cytokine. LAP is the TGF-beta pro-peptide that is cleaved intracellularly prior to secretion, and TGF-beta binds non-covalently to LAP. Formation of the large latent complex is important for the efficient secretion of TGF-beta. Previous studies have revealed that the LTBP-LAP interaction is mediated by intracellular exchange of a single disulphide bond within the third, and only the third, TB domain (TB3) with LAP. We have previously reported the structure of a homologous TB domain from fibrillin-1. However, TB3 contains a two amino acid insertion, not found in fibrillin-1 TB domains, which is not amenable to molecular modelling. In order to clarify the basis of TB domain function, we have determined the solution NMR structure of TB3(LTBP1). Comparison with the fibrillin-1 TB domain reveals that the two-residue insertion is associated with a significant increase in solvent accessibility of one of the disulphide bonds (linking the second and sixth cysteine residues). Site-directed mutagenesis and NMR studies indicate that this is the only disulphide bond that can be removed without perturbing the TB domain fold. Furthermore, a ring of negatively charged residues has been identified that surrounds this disulphide bond. Homology modelling suggests that the surface properties of TB3 domains from different LTBP isoforms correlate with binding activities. This research provides testable hypotheses regarding the molecular basis of complex formation between LTBPs and LAPs.
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(as it appears on PubMed at http://www.pubmed.gov), where 14607119 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14607119}}
==About this Structure==
==About this Structure==
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1KSQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KSQ OCA].
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1KSQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KSQ OCA].
==Reference==
==Reference==
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[[Category: Tb domain]]
[[Category: Tb domain]]
[[Category: Tgf-beta]]
[[Category: Tgf-beta]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:07:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:55:10 2008''

Revision as of 07:55, 2 July 2008

Image:1ksq.png

Template:STRUCTURE 1ksq

NMR Study of the Third TB Domain from Latent Transforming Growth Factor-beta Binding Protein-1

Template:ABSTRACT PUBMED 14607119

About this Structure

1KSQ is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Solution structure of the third TB domain from LTBP1 provides insight into assembly of the large latent complex that sequesters latent TGF-beta., Lack J, O'Leary JM, Knott V, Yuan X, Rifkin DB, Handford PA, Downing AK, J Mol Biol. 2003 Nov 21;334(2):281-91. PMID:14607119

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