PDBsum entry 4gxb

Protein transport/cell adhesion

PDB id: 4gxb

Contents

Protein chains

263 a.a.

15 a.a.

Ligands

GOL

Waters ×371

PDB id:

4gxb

Name:

Protein transport/cell adhesion

Title:

Structure of the snx17 atypical ferm domain bound to the npxy motif of p-selectin

Structure:

Sorting nexin-17. Chain: a. Fragment: ferm domain, unp residues 111-388. Synonym: snx17. Engineered: yes. P-selectin. Chain: b. Fragment: intracellular domain, unp residues 735-768. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: snx17. Expressed in: escherichia coli. Expression_system_taxid: 562. Mus musculus. Mouse. Organism_taxid: 10090.

Resolution:

1.80Å R-factor: 0.179 R-free: 0.204

Authors:

R.Ghai,A.Bugarcic,H.Liu,S.J.Norwood,S.S.Li,R.D.Teasdale,B.M.Collins

Key ref:

R.Ghai et al. (2013). Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins. Proc Natl Acad Sci U S A, 110, E643. PubMed id: 23382219 DOI: 10.1073/pnas.1216229110

Date:

04-Sep-12 Release date: 13-Mar-13

Protein chain

Q15036  (SNX17_HUMAN) -  Sorting nexin-17 from Homo sapiens

Seq: 470 a.a.

Struc: 263 a.a.

Protein chain

Q01102  (LYAM3_MOUSE) -  P-selectin from Mus musculus

Seq: 768 a.a.

Struc: 15 a.a.

Enzyme reactions

• Enzyme class: Chains A, B: E.C.?

DOI no: 10.1073/pnas.1216229110

Proc Natl Acad Sci U S A 110:E643 (2013)

PubMed id: 23382219

Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins.

R.Ghai, A.Bugarcic, H.Liu, S.J.Norwood, S.Skeldal, E.J.Coulson, S.S.Li, R.D.Teasdale, B.M.Collins.

ABSTRACT

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.