› 3rqf

X-ray diffraction
2.7Å resolution

Cerebral cavernous malformation 3 (CCM3) in complex with paxillin LD2

Released:
DOI: 10.2210/pdb3rqf/pdb
PDB entry 3rqf coloured by chain, front view.
PDB entry 3rqf coloured by chain, side view.
PDB entry 3rqf coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular recognition of leucine-aspartate repeat (LD) motifs by the focal adhesion targeting homology domain of cerebral cavernous malformation 3 (CCM3).
Li X, Ji W, Zhang R, Folta-Stogniew E, Min W, Boggon TJ
J Biol Chem 286 26138-47 (2011)
PMID: 21632544

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155831 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Programmed cell death protein 10 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 214 amino acids
Theoretical weight: 24.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BUL8 (Residues: 1-212; Coverage: 100%)
Gene names: CCM3, PDCD10, TFAR15
Sequence domains:
Structure domains:
Paxillin Chain: E
Molecule details ›
Chain: E
Length: 13 amino acids
Theoretical weight: 1.54 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P49023 (Residues: 141-153; Coverage: 2%)
Gene name: PXN

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P212121
Unit cell:
a: 62.862Å b: 115.469Å c: 124.379Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.237 0.291
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

15 review citations

Pericytes of the neurovascular unit: key functions and signaling pathways.
Sweeney et al. (2016)
14 more

1 mention without citation

Molecular recognition of leucine-aspartate repeat (LD) motifs by the focal adhesion targeting homology domain of cerebral cavernous malformation 3 (CCM3).
Li et al. (2011)