The entry DI1010105 describes the same interaction with the disordered partner bearing different post-translational modification(s).
Database Accession: DI1010103
Name: cAMP-dependent protein kinase catalytic subunit in complex with cAMP-dependent protein kinase inhibitor
PDB ID: 1cmk
Experimental method: X-ray (2.90 Å)
Source organism: Homo sapiens / Sus scrofa
Proof of disorder:
Primary publication of the structure:
Zheng J, Knighton DR, Xuong NH, Taylor SS, Sowadski JM, Ten Eyck LF
Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations.
(1993) Protein Sci. 2: 1559-73
PMID: 8251932
Abstract:
Three crystal structures, representing two distinct conformational states, of the mammalian catalytic subunit of cAMP-dependent protein kinase were solved using molecular replacement methods starting from the refined structure of the recombinant catalytic subunit ternary complex (Zheng, J., et al., 1993a, Biochemistry 32, 2154-2161). These structures correspond to the free apoenzyme, a binary complex with an iodinated inhibitor peptide, and a ternary complex with both ATP and the unmodified inhibitor peptide. The apoenzyme and the binary complex crystallized in an open conformation, whereas the ternary complex crystallized in a closed conformation similar to the ternary complex of the recombinant enzyme. The model of the binary complex, refined at 2.9 A resolution, shows the conformational changes associated with the open conformation. These can be described by a rotation of the small lobe and a displacement of the C-terminal 30 residues. This rotation of the small lobe alters the cleft interface in the active-site region surrounding the glycine-rich loop and Thr 197, a critical phosphorylation site. In addition to the conformational changes, the myristylation site, absent in the recombinant enzyme, was clearly defined in the binary complex. The myristic acid binds in a deep hydrophobic pocket formed by four segments of the protein that are widely dispersed in the linear sequence. The N-terminal 40 residues that lie outside the conserved catalytic core are anchored by the N-terminal myristylate plus an amphipathic helix that spans both lobes and is capped by Trp 30. Both posttranslational modifications, phosphorylation and myristylation, contribute directly to the stable structure of this enzyme.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown.Molecular function: not assigned
Biological process:
regulation of cell cycle process Any process that modulates a cellular process that is involved in the progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events.
Cellular component:
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: I, E
Notes: No modifications of the original PDB file.
Name: cAMP-dependent protein kinase inhibitor alpha
Source organism: Homo sapiens
Length: 22 residues
Sequence:Sequence according to PDB SEQRESTTYADFIASGRTGRRNAIHDIL
UniProtKB AC: P61925 (positions: 6-27) Coverage: 28.9%
UniRef90 AC: UniRef90_P61925 (positions: 6-27)
Name: cAMP-dependent protein kinase catalytic subunit alpha
Source organism: Sus scrofa
Length: 350 residues
Sequence:Sequence according to PDB SEQRESGNAAAAKKGSEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLVKHKETGNHFAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEYSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKDGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
UniProtKB AC: P36887 (positions: 2-351) Coverage: 99.7%
UniRef90 AC: UniRef90_P17612 (positions: 2-351)
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Chain I:
The 1-76 region described in DisProt entry DP00015 and the 1-32 region describen in IDEAL entry IID00349 cover 100% of the binding sequence in a homologous protein.
Chain E:
The protein kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00069). A solved monomeric structure of the domain is represented by PDB ID 1i09.
Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap). The structure can be rotated by left click and hold anywhere on the structure. Representation options can be edited by right clicking on the structure window.
