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TitleA structured interdomain linker directs self-polymerization of human uromodulin.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 113, Issue 6, Page 1552-1557, Year 2016
Publish dateFeb 9, 2016
AuthorsMarcel Bokhove / Kaoru Nishimura / Martina Brunati / Ling Han / Daniele de Sanctis / Luca Rampoldi / Luca Jovine /
PubMed AbstractUromodulin (UMOD)/Tamm-Horsfall protein, the most abundant human urinary protein, plays a key role in chronic kidney diseases and is a promising therapeutic target for hypertension. Via its bipartite ...Uromodulin (UMOD)/Tamm-Horsfall protein, the most abundant human urinary protein, plays a key role in chronic kidney diseases and is a promising therapeutic target for hypertension. Via its bipartite zona pellucida module (ZP-N/ZP-C), UMOD forms extracellular filaments that regulate kidney electrolyte balance and innate immunity, as well as protect against renal stones. Moreover, salt-dependent aggregation of UMOD filaments in the urine generates a soluble molecular net that captures uropathogenic bacteria and facilitates their clearance. Despite the functional importance of its homopolymers, no structural information is available on UMOD and how it self-assembles into filaments. Here, we report the crystal structures of polymerization regions of human UMOD and mouse ZP2, an essential sperm receptor protein that is structurally related to UMOD but forms heteropolymers. The structure of UMOD reveals that an extensive hydrophobic interface mediates ZP-N domain homodimerization. This arrangement is required for filament formation and is directed by an ordered ZP-N/ZP-C linker that is not observed in ZP2 but is conserved in the sequence of deafness/Crohn's disease-associated homopolymeric glycoproteins α-tectorin (TECTA) and glycoprotein 2 (GP2). Our data provide an example of how interdomain linker plasticity can modulate the function of structurally similar multidomain proteins. Moreover, the architecture of UMOD rationalizes numerous pathogenic mutations in both UMOD and TECTA genes.
External linksProc Natl Acad Sci U S A / PubMed:26811476 / PubMed Central
MethodsX-ray diffraction
Resolution2.251 - 3.2 Å
Structure data

PDB-4wrn:
Crystal structure of the polymerization region of human uromodulin/Tamm-Horsfall protein
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

PDB-5bup:
Crystal structure of the ZP-C domain of mouse ZP2
Method: X-RAY DIFFRACTION / Resolution: 2.251 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-ZN:
Unknown entry

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

Source
  • escherichia coli o157:h7 (bacteria)
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsSTRUCTURAL PROTEIN / ZP DOMAIN / EGF DOMAIN / EXTRACELLULAR MATRIX / GLYCOPROTEIN / CELL ADHESION / Sperm receptor / immunoglobulin-like domain / zona pellucida / protein polymerization

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