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
Replaces: 1T2GSummary for 2A4J
Entry DOI | 10.2210/pdb2a4j/pdb |
NMR Information | BMRB: 5992 |
Descriptor | Centrin 2, 17-mer peptide P1-XPC from DNA-repair protein complementing XP-C cells (2 entities in total) |
Functional Keywords | ef-hand, structural protein |
Biological source | Homo sapiens (human) More |
Cellular location | Cytoplasm, cytoskeleton, centrosome, centriole: P41208 Nucleus: Q96AX0 |
Total number of polymer chains | 2 |
Total formula weight | 11347.96 |
Authors | Yang, A.,Miron, S.,Mouawad, L.,Duchambon, P.,Blouquit, Y.,Craescu, C.T. (deposition date: 2005-06-29, release date: 2005-07-12, Last modification date: 2024-05-22) |
Primary citation | Yang, A.,Miron, S.,Mouawad, L.,Duchambon, P.,Blouquit, Y.,Craescu, C.T. Flexibility and plasticity of human centrin 2 binding to the xeroderma pigmentosum group C protein (XPC) from nuclear excision repair. Biochemistry, 45:3653-3663, 2006 Cited by PubMed Abstract: 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. PubMed: 16533048DOI: 10.1021/bi0524868 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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