DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. Proceedings of the National Academy of Sciences of the United States of America 2011 imex curation Jehle S., Vollmar BS., Bardiaux B., Dove KK., Rajagopal P., Gonen T., Oschkinat H., Klevit RE. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink weight by staining molecular weight estimation by staining weight by staining Jehle S., Vollmar BS., Bardiaux B., Dove KK., Rajagopal P., Gonen T., Oschkinat H., Klevit RE. DIP original experiment: DIP-249220X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. Proceedings of the National Academy of Sciences of the United States of America 2011 imex curation Jehle S., Vollmar BS., Bardiaux B., Dove KK., Rajagopal P., Gonen T., Oschkinat H., Klevit RE. Only protein-protein interactions ecolx Escherichia coli saxs x ray scattering saxs predetermined predetermined participant predetermined Jehle S., Vollmar BS., Bardiaux B., Dove KK., Rajagopal P., Gonen T., Oschkinat H., Klevit RE. DIP original experiment: DIP-249221X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. Proceedings of the National Academy of Sciences of the United States of America 2011 imex curation Jehle S., Vollmar BS., Bardiaux B., Dove KK., Rajagopal P., Gonen T., Oschkinat H., Klevit RE. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink weight by staining molecular weight estimation by staining weight by staining Jehle S., Vollmar BS., Bardiaux B., Dove KK., Rajagopal P., Gonen T., Oschkinat H., Klevit RE. DIP original experiment: DIP-249222X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. Proceedings of the National Academy of Sciences of the United States of America 2011 imex curation Jehle S., Vollmar BS., Bardiaux B., Dove KK., Rajagopal P., Gonen T., Oschkinat H., Klevit RE. Only protein-protein interactions ecolx Escherichia coli tem transmission electron microscopy tem predetermined predetermined participant predetermined Jehle S., Vollmar BS., Bardiaux B., Dove KK., Rajagopal P., Gonen T., Oschkinat H., Klevit RE. DIP original experiment: DIP-249224X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. Proceedings of the National Academy of Sciences of the United States of America 2011 imex curation Jehle S., Vollmar BS., Bardiaux B., Dove KK., Rajagopal P., Gonen T., Oschkinat H., Klevit RE. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink weight by staining molecular weight estimation by staining weight by staining Jehle S., Vollmar BS., Bardiaux B., Dove KK., Rajagopal P., Gonen T., Oschkinat H., Klevit RE. DIP original experiment: DIP-249223X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. cryab_human Alpha-crystallin B chain CRYAB CRYA2 Renal carcinoma antigen NY-REN-27 Alpha(B)-crystallin Rosenthal fiber component Heat shock protein beta-5 HSPB5 protein protein human Homo sapiens Human MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK DIP protein P02511 original sequence version: null AE08BED46B7849CB DIP protein P02511 original sequence version: 195 DIP protein P02511 original sequence version: 130 DIP protein P02511 original sequence version: 131 DIP protein P02511 original sequence version: 151 DIP protein P02511 original sequence version: 167 DIP protein P02511 original sequence version: 154 DIP protein P02511 original sequence version: 146 AE08BED46B7849CB cryab-10 1 6 unspecified role unspecified role unspecified role unspecified role P02511:p.Ala57Cys A57C mutation mutation certain certain sequence position certain certain certain sequence position certain A C This feature has been corrected as a result of our quality control procedures. The original label was 'A57C'. Wed May 02 17:32:24 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala57cys' Tue Jun 30 20:03:34 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala57Cys' ecolx Escherichia coli direct interaction direct interaction cryab-11 4 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction cryab-12 2 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction cryab-13 3 6 unspecified role unspecified role unspecified role unspecified role P02511:p.Ser59Cys S59C mutation mutation certain certain sequence position certain certain certain sequence position certain S C This feature has been corrected as a result of our quality control procedures. The original label was 'S59C'. Wed May 02 15:20:04 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser59cys' Tue Jun 30 16:46:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser59Cys' ecolx Escherichia coli direct interaction direct interaction cryab-14 5 6 unspecified role unspecified role unspecified role unspecified role P02511:p.Thr63Cys T63C mutation mutation certain certain sequence position certain certain certain sequence position certain T C This feature has been corrected as a result of our quality control procedures. The original label was 'T63C'. Wed May 02 16:58:41 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr63cys' Tue Jun 30 18:44:46 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr63Cys' ecolx Escherichia coli direct interaction direct interaction