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TitleProbing the Architecture of a Multi-PDZ Domain Protein: Structure of PDZK1 in Solution.
Journal, issue, pagesStructure, Vol. 26, Issue 11, Page 1522-11533.e5, Year 2018
Publish dateNov 6, 2018
AuthorsNelly R Hajizadeh / Joanna Pieprzyk / Petr Skopintsev / Ali Flayhan / Dmitri I Svergun / Christian Löw /
PubMed AbstractThe 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 ...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.
External linksStructure / PubMed:30220543
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution1.50332103817 Å
Structure data

SASDD85:
PDZK1 Domain 1-4 (Uncharacterized protein C1orf159)
Method: SAXS/SANS

PDB-6ezi:
PDZK1 domain 4 in complex with C-terminal peptide of human PepT2.
Method: X-RAY DIFFRACTION / Resolution: 1.50332103817 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsPROTEIN BINDING / PDZK1 Human peptide transporter Na(+)-H(+) exchange regulatory cofactor NHE-RF3 Protein complex binding

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