2A4J: Solution structure of the C-terminal domain (T94-Y172) of the human centrin 2 in complex with a 17 residues peptide (P1-XPC) from xeroderma pigmentosum group C protein

Human centrin 2 is a component of the nucleotide excision repair system, as a subunit of the heterotrimer including xeroderma pigmentosum group C protein (XPC) and hHR23B. The C-terminal domain of centrin (C-HsCen2) binds strongly a peptide from the XPC protein (P1-XPC: N(847)-R(863)). Here, we characterize the solution Ca(2+)-dependent structural and molecular features of the C-HsCen2 in complex with P1-XPC, mainly using NMR spectroscopy and molecular modeling. The N-terminal half of the peptide, organized as an alpha helix is anchored into a deep hydrophobic cavity of the protein, because of three bulky hydrophobic residues in position 1-4-8 and electrostatic contacts with the centrin helix E. Investigation of the whole centrin interactions shows that the N-terminal domain of the protein is not involved in the complex formation and is structurally independent from the peptide-bound C-terminal domain. The complex may exist in three different binding conformations corresponding to zero, one, and two Ca(2+)-bound states, which may exchange with various rates and have distinct structural stability. The various features of the intermolecular interaction presented here constitute a centrin-specific mode for the target binding.
PDB ID: 2A4JDownload
MMDB ID: 162331
PDB Deposition Date: 2005/6/29
Updated in MMDB: 2018/05
Experimental Method:
solution nmr
Source Organism:
Homo sapiens
Similar Structures:
Molecular Components in 2A4J
Label Count Molecule
Proteins (2 molecules)
Centrin 2(Gene symbol: CETN2)
Molecule annotation
17-mer Peptide P1-xpc From DNA-repair Protein Complementing Xp-c Cells
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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