General Information

The entry DI1100095 describes the same interaction with the disordered partner bearing different post-translational modification(s).

Database Accession: DI1100031

Name: cAMP-dependent protein kinase complexed with an unmodified PKI-alpha peptide

PDB ID: 1apm PDB

Experimental method: X-ray (2.00 Å)

Source organism: Mus musculus

Proof of disorder: Inferred from homology

Primary publication of the structure:

Knighton DR, Bell SM, Zheng J, Ten Eyck LF, Xuong NH, Taylor SS, Sowadski JM
2.0 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with a peptide inhibitor and detergent.
(1993) Acta Crystallogr. D Biol. Crystallogr. 49: 357-61

PMID: 15299526 PubMed

Abstract:

. A mutant (Serl39Ala) of the mouse recombinant catalytic (C) subunit of cAMP-dependent protein kinase was co-crystallized with a peptide inhibitor, PKI(5-24), and MEGA-8 (octanoyl-N-methylglucamide) detergent. This structure was refined using all observed data (30 248 reflections) between 30 and 1.95 A resolution to an R factor of 0.186. R.m.s. deviations of bond lengths and bond angles are 0.013 A and 2.3 degrees, respectively. The final model has 3075 atoms (207 solvent) with a mean B factor of 31.9 A(2). The placement of invariant protein-kinase residues and most C:PKI(5-24) interactions were confirmed, but register errors affecting residues 55-64 and 309-339 were corrected during refinement by shifting the affected sequences toward the C terminus along the previously determined backbone path. New details of C:PKI(5-24) interactions and the Ser338 autophosphorylation site are described, and the acyl group binding site near the catalytic subunit NH(2) terminus is identified.


Function and Biology Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown.

Molecular function:

protein kinase binding Interacting selectively and non-covalently with a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate. GeneOntology

protein kinase A binding Interacting selectively and non-covalently with any subunit of protein kinase A. GeneOntology

Biological process:

regulation of cellular process Any process that modulates the frequency, rate or extent of a cellular process, any of those that are carried out at the cellular level, but are not necessarily restricted to a single cell. For example, cell communication occurs among more than one cell, but occurs at the cellular level. GeneOntology

regulation of intracellular protein transport Any process that modulates the frequency, rate or extent of the directed movement of proteins within cells. GeneOntology

Cellular component:

nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. GeneOntology

cytoplasm All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GeneOntology

Structure Summary Structural annotations of the participating protein chains.

Entry contents: 2 distinct polypeptide molecules

Chains: I, E

Notes: No modifications of the original PDB file.

Chain I

Name: cAMP-dependent protein kinase inhibitor alpha Disordered Inferred from homology

Source organism: Mus musculus

Length: 20 residues

Sequence:Sequence according to PDB SEQRESTTYADFIASGRTGRRNAIHD

UniProtKB AC: P63248 (positions: 6-25) UniProt Coverage: 26.3%

UniRef90 AC: UniRef90_P63248 (positions: 6-25) UniRef90

Chain E

Name: cAMP-dependent protein kinase catalytic subunit alpha Ordered

Source organism: Mus musculus

Length: 341 residues

Sequence:Sequence according to PDB SEQRESSEQESVKEFLAKAKEDFLKKWETPSQNTAQLDQFDRIKTLGTGSFGRVMLVKHKESGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVAGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFTEF

UniProtKB AC: P05132 (positions: 11-351) UniProt Coverage: 97.2%

UniRef90 AC: UniRef90_P17612 (positions: 11-351) UniRef90

Evidence Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding.

Chain I: Disordered Inferred from homology

The corresponding region of a closely homologous protein has been shown to be disordered in the 1-76 region described in DisProt entry DP00015 (covers 100% of the sequence present in the structure).

Chain E: Ordered

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 4nts.

Related Structure(s) 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).

There are 24 related structures in the Protein Data Bank:



Domain Type:

Protein kinase







The molecule viewer shows the original PDB stucture.

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.

Download the original structure (.pdb)

Download this entry's XML file (.xml)