Database Accession: DI3000004
Name: C-terminal region of p21(WAF1/CIP1) complexed with human PCNA.
PDB ID: 1axc
Experimental method: X-ray (2.60 Å)
Source organism: Homo sapiens
Proof of disorder:
Kd: 8.80×10-08 M
Primary publication of the structure:
Gulbis JM, Kelman Z, Hurwitz J, O'Donnell M, Kuriyan J
Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA.
(1996) Cell 87: 297-306
PMID: 8861913
Abstract:
The crystal structure of the human DNA polymerase delta processivity factor PCNA (proliferating cell nuclear antigen) complexed with a 22 residue peptide derived from the C-terminus of the cell-cycle checkpoint protein p21(WAF1/CIP1) has been determined at 2.6 angstrom resolution. p21 binds to PCNA in a 1:1 stoichiometry with an extensive array of interactions that include the formation of a beta sheet with the interdomain connector loop of PCNA. An intact trimeric ring is maintained in the structure of the p21-PCNA complex, with a central hole available for DNA interaction. The ability of p21 to inhibit the action of PCNA is therefore likely to be due to its masking of elements on PCNA that are required for the binding of other components of the polymerase assembly.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
enzyme regulator activity Binds to and modulates the activity of an enzyme.
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.
protein complex binding Interacting selectively and non-covalently with any protein complex (a complex of two or more proteins that may include other nonprotein molecules).
Biological process:
DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest A cascade of processes induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, in response to the detection of DNA damage and resulting in the stopping or reduction in rate of the cell cycle.
regulation of nucleic acid-templated transcription Any process that modulates the frequency, rate or extent of nucleic acid-templated transcription.
regulation of cellular macromolecule biosynthetic process Any process that modulates the frequency, rate or extent of cellular macromolecule biosynthetic process.
epithelial cell differentiation The process in which a relatively unspecialized cell acquires specialized features of an epithelial cell, any of the cells making up an epithelium.
positive regulation of macromolecule metabolic process Any process that increases the frequency, rate or extent of the chemical reactions and pathways involving macromolecules, any molecule of high relative molecular mass, the structure of which essentially comprises the multiple repetition of units derived, actually or conceptually, from molecules of low relative molecular mass.
positive regulation of cellular metabolic process Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways by which individual cells transform chemical substances.
regulation of biological quality Any process that modulates a qualitative or quantitative trait of a biological quality. A biological quality is a measurable attribute of an organism or part of an organism, such as size, mass, shape, color, etc.
animal organ regeneration The regrowth of a lost or destroyed organ.
response to organonitrogen compound Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an organonitrogen stimulus. An organonitrogen compound is formally a compound containing at least one carbon-nitrogen bond.
Cellular component:
intracellular non-membrane-bounded organelle Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane and occurring within the cell. Includes ribosomes, the cytoskeleton and chromosomes.
Structural annotations of the participating protein chains.Entry contents: 4 distinct polypeptide molecules
Chains: B, A, C, E
Notes: Chains D and F were removed as chains A, B, C and E represent the biologically relevant interaction.
Name: Cyclin-dependent kinase inhibitor 1
Source organism: Homo sapiens
Length: 18 residues
Sequence:Sequence according to PDB SEQRESRQTSMTDFYHSKRRLIFS
UniProtKB AC: P38936 (positions: 143-160) Coverage: 11%
UniRef90 AC: UniRef90_P38936 (positions: 143-160)
Name: Proliferating cell nuclear antigen
Source organism: Homo sapiens
Length: 255 residues
Sequence:Sequence according to PDB SEQRESMFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNIKLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHLKYYLAPKI
UniProtKB AC: P12004 (positions: 1-255) Coverage: 97.7%
UniRef90 AC: UniRef90_P12004 (positions: 1-255)
Name: Proliferating cell nuclear antigen
Source organism: Homo sapiens
Length: 255 residues
Sequence:Sequence according to PDB SEQRESMFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNIKLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHLKYYLAPKI
UniProtKB AC: P12004 (positions: 1-255) Coverage: 97.7%
UniRef90 AC: UniRef90_P12004 (positions: 1-255)
Name: Proliferating cell nuclear antigen
Source organism: Homo sapiens
Length: 255 residues
Sequence:Sequence according to PDB SEQRESMFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNIKLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHLKYYLAPKI
UniProtKB AC: P12004 (positions: 1-255) Coverage: 97.7%
UniRef90 AC: UniRef90_P12004 (positions: 1-255)
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Chain B:
The 1-164 region described in DisProt entry DP00016 and in IDEAL entry IID00043 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains four known functional linear motifs (DEG_CRL4_CDT2_1, DOC_CYCLIN_1, LIG_PCNA_PIPBox_1, TRG_NLS_Bipartite_1) and a known modification site (MOD_PKB_1).
Chain A:
PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID: 8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1w60.
Chain C:
PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID: 8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1w60.
Chain E:
PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID: 8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1w60.
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.
Download our modified structure (.pdb)
