Solution structure of the link module: a hyaluronan-binding domain involved in extracellular matrix stability and cell migration
Article Abstract:
The solution structure of hyaluronan-binding domains in proteins called Link modules, also known as proteoglycan tandem repeat, isolated from human TSG-6 was determined by nuclear magnetic resonance spectroscopy. Two alpha helices and two antiparallel beta sheets arranged in a compact fold with a flattened shape was observed surrounding a hydrophobic core composed of side chains from 21 amino acids. The Link module shared a high similarity with the structure of the C-type lectin domain of human mannose-binding protein C-chain and was suggested to be involved in cell migration.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding
Article Abstract:
Biochemical evidence indicates that a polypeptide segment at the amino terminus of P-selectin glycoprotein ligand 1 (PSGL-1) is essential for high-affinity P-selectin binding on the surface of myeloid cells. The noncarbohydrate anionic segment consists of 19 amino acids and contains at least one sulfated tyrosine residue, where the P-selectin binding site needed to promote PSGL-1-P-selectin interaction is located.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20
Article Abstract:
The binding of mitochondrial presequences to the mitochondrial membrane occurs via hydrophobic rather than ionic interactions. The presequence forms an amphiphilic helical structure with hydrophobic leucines that interact with a hydrophobic patch in the receptor groove.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2000
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