PDBsum entry 4g69

Membrane protein/signaling protein

PDB id

4g69

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Contents

			Protein chain

					97 a.a.

			Ligands

					TYR-LEU-VAL-THR- SER-VAL

			Waters ×106

PDB id:

4g69

Links

Name:

Membrane protein/signaling protein

Title:

Structure of the human discs large 1 pdz2 - adenomatous polyposis coli cytoskeletal polarity complex

Structure:

Disks large homolog 1. Chain: a. Fragment: pdz2, unp residues 310-407. Synonym: synapse-associated protein 97, sap-97, sap97, hdlg. Engineered: yes. Adenomatous polyposis coli protein. Chain: b. Fragment: apc c-terminal peptide, unp residues 2833-2843. Synonym: protein apc, deleted in polyposis 2.5.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: dlg1. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Other_details: adenomatous polyposis coli (apc) c-terminal 11 residues synthesized with n-terminal tetramethyl rhodamine tag

Resolution:

2.00Å

R-factor:

0.172

R-free:

0.183

Authors:

K.C.Slep

Key ref:

K.C.Slep (2012). Structure of the human discs large 1 PDZ2- adenomatous polyposis coli cytoskeletal polarity complex: insight into peptide engagement and PDZ clustering. Plos One, 7, e50097. PubMed id: 23185543

Date:

18-Jul-12

Release date:

12-Dec-12

PROCHECK

	Headers

	References

Protein chain

Q12959 (DLG1_HUMAN) - Disks large homolog 1 from Homo sapiens

Seq: Struc:

Seq: Struc:					904 a.a. 97 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

	Plos One 7:e50097 (2012)
PubMed id: 23185543

Structure of the human discs large 1 PDZ2- adenomatous polyposis coli cytoskeletal polarity complex: insight into peptide engagement and PDZ clustering.
K.C.Slep.

ABSTRACT

The membrane associated guanylate kinase (MAGUK) family member, human Discs Large 1 (hDlg1) uses a PDZ domain array to interact with the polarity determinant, the Adenomatous Polyposis Coli (APC) microtubule plus end binding protein. The hDLG1-APC complex mediates a dynamic attachment between microtubule plus ends and polarized cortical determinants in epithelial cells, stem cells, and neuronal synapses. Using its multi-domain architecture, hDlg1 both scaffolds and regulates the polarity factors it engages. Molecular details underlying the hDlg1-APC interaction and insight into how the hDlg1 PDZ array may cluster and regulate its binding factors remain to be determined. Here, I present the crystal structure of the hDlg1 PDZ2-APC complex and the molecular determinants that mediate APC binding. The hDlg1 PDZ2-APC complex also provides insight into potential modes of ligand-dependent PDZ domain clustering that may parallel Dlg scaffold regulatory mechanisms. The hDlg1 PDZ2-APC complex presented here represents a core biological complex that bridges polarized cortical determinants with the dynamic microtubule cytoskeleton.