A structural screen for candidate polyphosphate binding surfaces in human membrane associated proteins
Inorganic polyphosphate (polyP) can alter protein function through noncovalent binding, yet its partners among human membrane associated proteins remain poorly characterized. PolyP is recognized through two modes: a structure-based mode driven by charge complementarity with sites assembled by protein folding, and a more recently defined sequence-based mode at histidine and lysine rich tracts. The…
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