Pleckstrin homology domain, spectrin-type
IPR001605
Definition
Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane; it associates with band 4.1 and actin to form the cytoskeletal super-structure. The native spectrin molecule is a tetramer comprising two anti-parallel heterodimers joined head to head, such that the C terminus of the alpha-subunit and the N terminus of the beta-subunit are included within the same molecule. Spectrin is similar to alpha-actinin and dystrophin, and contains a pleckstrin homology (PH) domain. The exact function of the PH domain is unknown, but evidence suggests that it contains an electrostatically-polarised pocket that facilitates binding of a ligand (e.g., a peptide). The PH domain contains a number of hydrophobic residues that form a hydrophobic core responsible for protein stability. The spectrin PH domain PMID:8208297, which has the familiar 7-stranded anti-parallel up and down β-barrel capped by a C-terminal amphiphilic α helical cap PMID:8208296, contains insertions that confer 2 additional turns of α-helix in the loop between strands 3 and 4. The C-terminal helix is packed into a gorge between strands 1 and 2, and lies parallel to strand 7 PMID:8599766.
6 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
Loading the interactive Seroatlas explorer...