Solution structure of the third TB domain from LTBP1 provides insight into assembly of the large latent complex that sequesters latent TGF-beta.
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-bet...
Main Authors: | Lack, J, O'Leary, J, Knott, V, Yuan, X, Rifkin, D, Handford, P, Downing, A |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2003
|
Similar Items
-
Immunochemical study of fibrillin-2 and LTBP-2 (latent TGF-b binding protein) in bovine intervertebral disc
by: Li, B, et al.
Published: (2011) -
Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
by: Rudd, P, et al.
Published: (2000) -
Effects of the N2144S mutation on backbone dynamics of a TB-cbEGF domain pair from human fibrillin-1.
by: Yuan, X, et al.
Published: (2002) -
Prevalence of Latent TB and Effectiveness of BCG Vaccination Against Latent Tuberculosis: An Observational Study
by: Birger Trollfors, MD, et al.
Published: (2021-08-01) -
Latent TGF-beta binding protein-1 plays an important role in craniofacial development
by: Yiting Xiong, et al.
Published: (2020-11-01)