 |
PDBsum entry 1lsl
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Cell adhesion
|
PDB id
|
|
|
|
1lsl
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structure of the tsp-1 type 1 repeats: a novel layered fold and its biological implication.
|
|
|
Authors
|
|
K.Tan,
M.Duquette,
J.H.Liu,
Y.Dong,
R.Zhang,
A.Joachimiak,
J.Lawler,
J.H.Wang.
|
|
|
Ref.
|
|
J Cell Biol, 2002,
159,
373-382.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Thrombospondin-1 (TSP-1) contains three type 1 repeats (TSRs), which mediate
cell attachment, glycosaminoglycan binding, inhibition of angiogenesis,
activation of TGFbeta, and inhibition of matrix metalloproteinases. The crystal
structure of the TSRs reported in this article reveals a novel, antiparallel,
three-stranded fold that consists of alternating stacked layers of tryptophan
and arginine residues from respective strands, capped by disulfide bonds on each
end. The front face of the TSR contains a right-handed spiral, positively
charged groove that might be the "recognition" face, mediating interactions with
various ligands. This is the first high-resolution crystal structure of a TSR
domain that provides a prototypic architecture for structural and functional
exploration of the diverse members of the TSR superfamily.
|
|
|
|
|
|
|
