6EZI

PDZK1 domain 4 in complex with C-terminal peptide of human PepT2.

Summary for 6EZI

• Entry DOI: 10.2210/pdb6ezi/pdb
• Descriptor: Na(+)/H(+) exchange regulatory cofactor NHE-RF3, Solute carrier family 15 member 2, GLYCEROL, ... (4 entities in total)
• Functional Keywords: pdzk1 human peptide transporter na(+)-h(+) exchange regulatory cofactor nhe-rf3 protein complex binding, protein binding
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 10950.71

Authors

Loew, C.,Flayhan, A.,Pieprzyk, J. (deposition date: 2017-11-15, release date: 2018-09-26, Last modification date: 2024-01-17)

Primary citation

Hajizadeh, N.R.,Pieprzyk, J.,Skopintsev, P.,Flayhan, A.,Svergun, D.I.,Low, C.
Probing the Architecture of a Multi-PDZ Domain Protein: Structure of PDZK1 in Solution.
Structure, 26:1522-1533.e5, 2018

PubMed Abstract: The scaffolding protein PDZK1 has been associated with the regulation of membrane transporters. It contains four conserved PDZ domains, which typically recognize a 3-5-residue long motif at the C terminus of the binding partner. The atomic structures of the individual domains are available but their spatial arrangement in the full-length context influencing the binding properties remained elusive. Here we report a systematic study of full-length PDZK1 and deletion constructs using small-angle X-ray scattering, complemented with biochemical and functional studies on PDZK1 binding to known membrane protein partners. A hybrid modeling approach utilizing multiple scattering datasets yielded a well-defined, extended, asymmetric L-shaped domain organization of PDZK1 in contrast to a flexible "beads-on-string" model predicted by bioinformatics analysis. The linker regions of PDZK1 appear to play a central role in the arrangement of the four domains underlying the importance of studying scaffolding proteins in their full-length context.

PubMed: 30220543
DOI: 10.1016/j.str.2018.07.016

Experimental method

X-RAY DIFFRACTION (1.50332103817 Å)