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Together with PLTP, CETP, BPI, and LBP, the PLUNC proteins form a superfamily known as the lipid transfer/lipopolysaccharide binding protein (LT/LBP) family, whose members share the ability to bind a variety of lipid substrates.
Various lineages have acquired an amino acid binding domain known as the ACT domain (pfam01842), which is known to bind a variety of amino acids, thus functioning as an allosteric domain for many proteins including phosphoglycerate dehydrogenase, aspartokinase, acetolactate synthase, phenylalanine hydroxylase, prephenate dehydratase and formyltetrahydrofolate deformylase.
It can bind a variety of guest molecules inside their torus-shaped cavities and serve as a model host site.
Infected erythrocytes bind a variety of host receptors but certain adhesion traits are associated with more severe disease.
Macrocyclic Lewis acidic hosts with structures incorporating electron-withdrawing icosahedral carboranes and electrophilic mercury centers bind a variety of electron-rich guests.
Clonable tags localization has been achieved via metallothionein, a small cysteine-rich protein that can bind a variety of heavy metal ions with its cysteine residues (Hamer 1986; Kagi and Schaffer 1988; Mercogliano and DeRosier 2007).
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Tenascin-X is an extracellular matrix protein and binds a variety of molecules in extracellular matrix and on cell membrane.
DFsc stoichiometrically binds a variety of divalent metal ions, including Zn II), Co II), Fe(II), and Mn II), with micromolar affinities.
EhCaBP1 is also thought to be involved in multiple pathways as it binds a variety of target proteins observed by immunoprecipitation and mass-spectrometric studies [5, unpublished observation].
More recently, it was demonstrated that DARC binds a variety of CXC and CC chemokines [ 4- 7].
CCR3 binds a variety of C-C chemokines one of which is CCL11 (formerly known as eotaxin).
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