Unknown

Dataset Information

0

Solution NMR structures of immunoglobulin-like domains 7 and 12 from obscurin-like protein 1 contribute to the structural coverage of the Human Cancer Protein Interaction Network.


ABSTRACT: High-quality solution NMR structures of immunoglobulin-like domains 7 and 12 from human obscurin-like protein 1 were solved. The two domains share 30% sequence identity and their structures are, as expected, rather similar. The new structures contribute to structural coverage of human cancer associated proteins. Mutations of Arg 812 in domain 7 cause the rare 3-M syndrome, and this site is located in a surface area predicted to be involved in protein-protein interactions.

SUBMITTER: Pulavarti SV 

PROVIDER: S-EPMC4945113 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Solution NMR structures of immunoglobulin-like domains 7 and 12 from obscurin-like protein 1 contribute to the structural coverage of the Human Cancer Protein Interaction Network.

Pulavarti Surya V S R K SV   Huang Yuanpeng J YJ   Pederson Kari K   Acton Thomas B TB   Xiao Rong R   Everett John K JK   Prestegard James H JH   Montelione Gaetano T GT   Szyperski Thomas T  

Journal of structural and functional genomics 20140703 4


High-quality solution NMR structures of immunoglobulin-like domains 7 and 12 from human obscurin-like protein 1 were solved. The two domains share 30% sequence identity and their structures are, as expected, rather similar. The new structures contribute to structural coverage of human cancer associated proteins. Mutations of Arg 812 in domain 7 cause the rare 3-M syndrome, and this site is located in a surface area predicted to be involved in protein-protein interactions. ...[more]

Similar Datasets

| S-EPMC2788292 | biostudies-literature
| S-EPMC4239167 | biostudies-literature
| S-EPMC3982801 | biostudies-literature
| S-EPMC9302192 | biostudies-literature
| S-EPMC9592556 | biostudies-literature
| S-EPMC3609422 | biostudies-literature
| S-EPMC4427657 | biostudies-literature
| S-EPMC4568557 | biostudies-literature
| S-EPMC6423719 | biostudies-literature