PDBsum entry 7d8h

Protein binding

PDB id: 7d8h

Contents

Protein chain

230 a.a.

Ligands

GLY-GLY-SEP-LEU-PRO-ASN

Waters ×37

PDB id:

7d8h

Name:

Protein binding

Title:

Crtc1 pser64 peptide in complex with 14-3-3 zeta

Structure:

14-3-3 protein zeta/delta. Chain: a. Synonym: protein kinasE C inhibitor protein 1,kcip-1. Engineered: yes. Crtc1 pser64 peptide. Chain: b. Synonym: creb-regulated transcription coactivator 1,mucoepidermoid carcinoma translocated protein 1,transducer of regulated camp response element-binding protein 1,transducer of creb protein 1.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ywhaz. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 9606

Resolution:

2.42Å R-factor: 0.213 R-free: 0.246

Authors:

H.Chen,H.Zhang,S.Xiang

Key ref:

H.Chen et al. (2021). Structural Insights into the Interaction Between CRTCs and 14-3-3. J Mol Biol, 433, 166874. PubMed id: 33556406 DOI: 10.1016/j.jmb.2021.166874

Date:

08-Oct-20 Release date: 24-Feb-21

Protein chain

P63104  (1433Z_HUMAN) -  14-3-3 protein zeta/delta from Homo sapiens

Seq: 245 a.a.

Struc: 230 a.a.

DOI no: 10.1016/j.jmb.2021.166874

J Mol Biol 433:166874 (2021)

PubMed id: 33556406

Structural Insights into the Interaction Between CRTCs and 14-3-3.

H.Chen, H.Zhang, P.Chen, S.Xiang.

ABSTRACT

The CREB-Regulated Transcriptional Coactivators (CRTCs) regulate the transcription of CREB target genes and have important functions in many biological processes. At the basal state, they are phosphorylated at multiple residues, which promotes their association with 14-3-3 that sequesters them in the cytoplasm. Upon dephosphorylation, they translocate into the nuclei and associate with CREB to activate the target gene transcription. Although three conserved serine residues in CRTCs have been implicated in their phosphorylation regulation, whether and how they mediate interactions with 14-3-3 is unclear. Here, we provide direct evidence that these residues and flanking regions interact with 14-3-3 and the structural basis of the interaction. Our study also identified a novel salt bridge in CRTC1 with an important function in binding 14-3-3, expanding the understanding of the interaction between 14-3-3 and its ligands.