› 4lmm

X-ray diffraction
1.1Å resolution

Crystal structure of NHERF1 PDZ1 domain complexed with the CXCR2 C-terminal tail in P21 space group

Released:
DOI: 10.2210/pdb4lmm/pdb
PDB entry 4lmm coloured by chain, front view.
PDB entry 4lmm coloured by chain, side view.
PDB entry 4lmm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
New conformational state of NHERF1-CXCR2 signaling complex captured by crystal lattice trapping.
Jiang Y, Lu G, Trescott LR, Hou Y, Guan X, Wang S, Stamenkovich A, Brunzelle J, Sirinupong N, Li C, Yang Z
OpenAccess logo PLoS One 8 e81904 (2013)
PMID: 24339979

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127084 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Na(+)/H(+) exchange regulatory cofactor NHE-RF1 Chain: A
Molecule details ›
Chain: A
Length: 91 amino acids
Theoretical weight: 9.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O14745 (Residues: 11-99; Coverage: 25%)
Gene names: NHERF, NHERF1, SLC9A3R1
Sequence domains: PDZ domain
Structure domains: Pdz3 Domain

Ligands and Environments

2 bound ligands:
Ligand ACY 1 x ACY
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P21
Unit cell:
a: 26.593Å b: 45.509Å c: 33.446Å
α: 90° β: 109.71° γ: 90°
R-values:
R R work R free
0.19 0.188 0.217
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

New roles of the Na+/H+ exchange regulatory factor 1 scaffolding protein: a review.
Bushau-Sprinkle et al. (2020)
5 other articles

1 mention without citation

Parathyroid hormone initiates dynamic NHERF1 phosphorylation cycling and conformational changes that regulate NPT2A-dependent phosphate transport.
Zhang et al. (2019)