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Cross-talk among structural domains of human DBP upon binding 25-hydroxyvitamin D.

Abstract：

:Serum vitamin D-binding protein (DBP) is structurally very similar to serum albumin (ALB); both have three distinct structural domains and high cysteine-content. Yet, functionally they are very different. DBP possesses high affinity for vitamin D metabolites and G-actin, but ALB does not. It has been suggested that there may be cross-talk among the domains so that binding of one ligand may influence the binding of others. In this study we have employed 2-p-toluidinyl-6-sulfonate (TNS), a reporter molecule that fluoresces upon binding to hydrophobic pockets of DBP. We observed that recombinant domain III possesses strong binding for TNS, which is not influenced by 25-hydroxyvitamin D(3) (25-OH-D(3)), yet TNS fluorescence of the whole protein is quenched by 25-OH-D(3). These results provide a direct evidence of cross-talk among the structural domains of DBP.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Ray A,Swamy N,Ray R

doi

10.1016/j.bbrc.2007.11.033

subject

Has Abstract

pub_date

2008-01-25 00:00:00

pages

746-50

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(07)02441-2

journal_volume

365

pub_type

杂志文章

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