Literature DB >> 23494870

Backbone ¹H, ¹³C and ¹⁵N resonance assignment of the C-terminal EGF-cbEGF pair of LTBP1 and flanking residues.

Ian B Robertson1, Penny A Handford, Christina Redfield.   

Abstract

Latent TGFβ binding protein 1 (LTBP1) is a large extracellular protein that has been shown to bind covalently to the propeptide of TGFβ cytokines and form a large latent complex, which is then incapable of binding TGFβ receptors. LTBP1 has also been demonstrated to interact with a number of insoluble extracellular matrix components, such as fibrillin, which may play a role in TGFβ regulation. Here we present the backbone (1)H, (13)C and (15)N assignments for two EGF domains of human LTBP1, and flanking regions, together forming a 12 kDa protein fragment at the C-terminus of LTBP1. This region is of particular interest as it is postulated to be involved in interactions with fibrillin microfibrils.

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Year:  2013        PMID: 23494870     DOI: 10.1007/s12104-013-9474-6

Source DB:  PubMed          Journal:  Biomol NMR Assign        ISSN: 1874-270X            Impact factor:   0.746


  3 in total

1.  NMR spectroscopic and bioinformatic analyses of the LTBP1 C-terminus reveal a highly dynamic domain organisation.

Authors:  Ian B Robertson; Penny A Handford; Christina Redfield
Journal:  PLoS One       Date:  2014-01-29       Impact factor: 3.240

2.  The N-Terminal Region of Fibrillin-1 Mediates a Bipartite Interaction with LTBP1.

Authors:  Ian B Robertson; Hans F Dias; Isabelle H Osuch; Edward D Lowe; Sacha A Jensen; Christina Redfield; Penny A Handford
Journal:  Structure       Date:  2017-06-29       Impact factor: 5.006

3.  Latent TGF-beta binding protein-1 plays an important role in craniofacial development.

Authors:  Yiting Xiong; Rongrong Sun; Jingyu Li; Yue Wu; Jingju Zhang
Journal:  J Appl Oral Sci       Date:  2020-11-04       Impact factor: 2.698

  3 in total

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