1r2a A: PDB entry domain

SCOP classification

• Root: SCOP hierarchy in SUPERFAMILY [ 0] (11)
• Class: All alpha proteins [ 46456] (284)
• Fold: Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit [ 47390]
• Superfamily: Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit [ 47391]
• Family: Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit [ 47392] (2)
• Protein:
  • cAMP-dependent protein kinase type II regulatory subunit [47393]
• PDB Entry Domain:
  • 1r2a A: [ 16995]
  • SUPERFAMILY domain annotation for 1r2aa
  • PDB structure summary for 1r2a

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InterPro annotation

• Cross references: IPR003117 SSF47391 Protein matches
• Abstract:

  In the absence of cAMP, Protein Kinase A (PKA) exists as an equimolar tetramer of regulatory (R) and catalytic (C) subunits [11734894]. In addition to its role as an inhibitor of the C subunit, the R subunit anchors the holoenzyme to specific intracellular locations and prevents the C subunit from entering the nucleus. All R subunits have a conserved domain structure consisting of the N-terminal dimerization domain, inhibitory region, cAMP-binding domain A and cAMP-binding domain B. R subunits interact with C subunits primarily through the inhibitory site. The cAMP-binding domains show extensive sequence similarity and bind cAMP cooperatively.

  Two types of R subunit exist - Type I and Type II - which differ in molecular weight, sequence, autophosphorylation cabaility, cellular location and tissue distribution. Types I and II were further sub-divided into alpha and beta subtypes, based mainly on sequence similarity. This family of RII alpha, the regulatory subunit portion of type II PKA proteins, contains the dimerisation interface and binding site for A-kinase-anchoring proteins (AKAPs).

InterPro database

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