Cargando…
The NMR structure of the murine DLC2 SAM domain reveals a variant fold that is similar to a four-helix bundle
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 understandin...
Autores principales: | , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2007
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1899508/ https://www.ncbi.nlm.nih.gov/pubmed/17519008 http://dx.doi.org/10.1186/1472-6807-7-34 |
_version_ | 1782133946599866368 |
---|---|
author | Kwan, Jamie J Donaldson, Logan W |
author_facet | Kwan, Jamie J Donaldson, Logan W |
author_sort | Kwan, Jamie J |
collection | PubMed |
description | 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. |
format | Text |
id | pubmed-1899508 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-18995082007-06-27 The NMR structure of the murine DLC2 SAM domain reveals a variant fold that is similar to a four-helix bundle Kwan, Jamie J Donaldson, Logan W BMC Struct Biol Research Article 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. BioMed Central 2007-05-22 /pmc/articles/PMC1899508/ /pubmed/17519008 http://dx.doi.org/10.1186/1472-6807-7-34 Text en Copyright © 2007 Kwan and Donaldson; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Kwan, Jamie J Donaldson, Logan W The NMR structure of the murine DLC2 SAM domain reveals a variant fold that is similar to a four-helix bundle |
title | The NMR structure of the murine DLC2 SAM domain reveals a variant fold that is similar to a four-helix bundle |
title_full | The NMR structure of the murine DLC2 SAM domain reveals a variant fold that is similar to a four-helix bundle |
title_fullStr | The NMR structure of the murine DLC2 SAM domain reveals a variant fold that is similar to a four-helix bundle |
title_full_unstemmed | The NMR structure of the murine DLC2 SAM domain reveals a variant fold that is similar to a four-helix bundle |
title_short | The NMR structure of the murine DLC2 SAM domain reveals a variant fold that is similar to a four-helix bundle |
title_sort | nmr structure of the murine dlc2 sam domain reveals a variant fold that is similar to a four-helix bundle |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1899508/ https://www.ncbi.nlm.nih.gov/pubmed/17519008 http://dx.doi.org/10.1186/1472-6807-7-34 |
work_keys_str_mv | AT kwanjamiej thenmrstructureofthemurinedlc2samdomainrevealsavariantfoldthatissimilartoafourhelixbundle AT donaldsonloganw thenmrstructureofthemurinedlc2samdomainrevealsavariantfoldthatissimilartoafourhelixbundle AT kwanjamiej nmrstructureofthemurinedlc2samdomainrevealsavariantfoldthatissimilartoafourhelixbundle AT donaldsonloganw nmrstructureofthemurinedlc2samdomainrevealsavariantfoldthatissimilartoafourhelixbundle |