4GXB: Structure of the Snx17 Atypical Ferm Domain Bound to the Npxy Motif of P-selectin

Transit of proteins through the endosomal organelle following endocytosis is critical for regulating the homeostasis of cell-surface proteins and controlling signal transduction pathways. However, the mechanisms that control these membrane-transport processes are poorly understood. The Phox-homology (PX) domain-containing proteins sorting nexin (SNX) 17, SNX27, and SNX31 have emerged recently as key regulators of endosomal recycling and bind conserved Asn-Pro-Xaa-Tyr-sorting signals in transmembrane cargos via an atypical band, 4.1/ezrin/radixin/moesin (FERM) domain. Here we present the crystal structure of the SNX17 FERM domain bound to the sorting motif of the P-selectin adhesion protein, revealing both the architecture of the atypical FERM domain and the molecular basis for recognition of these essential sorting sequences. We further show that the PX-FERM proteins share a promiscuous ability to bind a wide array of putative cargo molecules, including receptor tyrosine kinases, and propose a model for their coordinated molecular interactions with membrane, cargo, and regulatory proteins.
PDB ID: 4GXBDownload
MMDB ID: 108301
PDB Deposition Date: 2012/9/4
Updated in MMDB: 2013/03
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Mus musculus
Similar Structures:
Biological Unit for 4GXB: dimeric; determined by author and by software (PISA)
Molecular Components in 4GXB
Label Count Molecule
Proteins (2 molecules)
Sorting Nexin-17
Molecule annotation
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB