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3DRZ

X-ray crystal structure of the N-terminal BTB domain of human KCTD5 protein

Summary for 3DRZ
Entry DOI10.2210/pdb3drz/pdb
Related3DRX 3DRY
DescriptorBTB/POZ domain-containing protein KCTD5 (2 entities in total)
Functional Keywordskctd5, btb/poz, potassium channel domain t1, pentamer, unknown function
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm, cytosol: Q9NXV2
Total number of polymer chains5
Total formula weight61604.84
Authors
Tereshko, V.,Dementieva, I.,Goldstein, S.A.N. (deposition date: 2008-07-11, release date: 2009-02-17, Last modification date: 2024-11-13)
Primary citationDementieva, I.S.,Tereshko, V.,McCrossan, Z.A.,Solomaha, E.,Araki, D.,Xu, C.,Grigorieff, N.,Goldstein, S.A.
Pentameric assembly of potassium channel tetramerization domain-containing protein 5.
J.Mol.Biol., 387:175-191, 2009
Cited by
PubMed Abstract: We report the X-ray crystal structure of human potassium channel tetramerization domain-containing protein 5 (KCTD5), the first member of the family to be so characterized. Four findings were unexpected. First, the structure reveals assemblies of five subunits while tetramers were anticipated; pentameric stoichiometry is observed also in solution by scanning transmission electron microscopy mass analysis and analytical ultracentrifugation. Second, the same BTB (bric-a-brac, tramtrack, broad complex) domain surface mediates the assembly of five KCTD5 and four voltage-gated K(+) (Kv) channel subunits; four amino acid differences appear crucial. Third, KCTD5 complexes have well-defined N- and C-terminal modules separated by a flexible linker that swivels by approximately 30 degrees; the C-module shows a new fold and is required to bind Golgi reassembly stacking protein 55 with approximately 1 microM affinity, as judged by surface plasmon resonance and ultracentrifugation. Fourth, despite the homology reflected in its name, KCTD5 does not impact the operation of Kv4.2, Kv3.4, Kv2.1, or Kv1.2 channels.
PubMed: 19361449
DOI: 10.1016/j.jmb.2009.01.030
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

227344

数据于2024-11-13公开中

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