The NMR structure of the murine DLC2 SAM domain reveals a variant fold that is similar to a four-helix bundle.
BMC Struct Biol
; 7: 34, 2007 May 22.
Article
em En
| MEDLINE
| ID: mdl-17519008
ABSTRACT
BACKGROUND:
The tumor suppressor DLC2 (Deleted in Liver Cancer -2) participates in cell signaling at the mitochondrial membrane. DLC2 is characterized by a SAM (sterile alpha motif) domain, a Rho GTPase activating protein (GAP) domain, and a START lipid transfer domain.RESULTS:
Towards understanding the function of DLC2, we have solved the NMR solution structure of the SAM domain. The DLC2-SAM domain structure reveals an atypical four-helix composition that is distinct from the five-helix SAM domain structures that have been determined to date. From structural alignments, helix 3 of the canonical SAM domain appears to be replaced by shorter, extended secondary structure that follows a similar path. Another difference is demonstrated by helices 1 and 2 that form a helical hairpin that is situated approximately parallel to the canonical helix 5.CONCLUSION:
The DLC2-SAM domain adopts a structure that is topologically more similar to an anti-parallel four-helix bundle than a canonical SAM domain. This alternate topology may allow the DLC2-SAM domain to interact with a novel set of ligands.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Ressonância Magnética Nuclear Biomolecular
/
Estrutura Quaternária de Proteína
/
Proteínas Supressoras de Tumor
Limite:
Animals
Idioma:
En
Revista:
BMC Struct Biol
Assunto da revista:
BIOLOGIA
Ano de publicação:
2007
Tipo de documento:
Article