Crystallization and preliminary X-ray diffraction data of the complex between human centrin 2 and a peptide from the protein XPC.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 62(Pt 7): 649-51, 2006 Jul 01.
Article
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| MEDLINE
| ID: mdl-16820684
ABSTRACT
Centrins are highly conserved calcium-binding proteins involved in the nucleotide-excision repair pathway as a subunit of the heterotrimer including the XPC and hHR23B proteins. A complex formed by a Ca2+-bound human centrin 2 construct (the wild type lacking the first 25 amino acids) with a 17-mer peptide derived from the XPC sequence (residues Asn847-Arg863) was crystallized. Data were collected to 1.65 angstroms resolution from crystals grown in 30% monomethyl polyethylene glycol (MPEG) 500, 100 mM NaCl and 100 mM Bicine pH 9.0. Crystals are monoclinic and belong to space group C2, with two molecules in the asymmetric unit. The unit-cell parameters are a = 60.28, b = 59.42, c = 105.14 angstroms, alpha = gamma = 90, beta = 94.67 degrees. A heavy-atom derivative was obtained by co-crystallization with Sr2+. The substitution was rationalized by calorimetry experiments, which indicate a binding constant for Sr2+ of 4.0 x 10(4) M(-1).
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas de Unión al Calcio
/
Proteínas de Ciclo Celular
/
Proteínas de Unión al ADN
Límite:
Humans
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Año:
2006
Tipo del documento:
Article
País de afiliación:
Francia