1JBI
NMR structure of the LCCL domain
Summary for 1JBI
| Entry DOI | 10.2210/pdb1jbi/pdb |
| NMR Information | BMRB: 5047 |
| Descriptor | cochlin (1 entity in total) |
| Functional Keywords | alpha-beta protein, structural genomics, unknown function |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted, extracellular space, extracellular matrix: O43405 |
| Total number of polymer chains | 1 |
| Total formula weight | 10609.98 |
| Authors | Liepinsh, E.,Trexler, M.,Kaikkonen, A.,Weigelt, J.,Banyai, L.,Patthy, L.,Otting, G. (deposition date: 2001-06-05, release date: 2001-10-17, Last modification date: 2024-10-30) |
| Primary citation | Liepinsh, E.,Trexler, M.,Kaikkonen, A.,Weigelt, J.,Banyai, L.,Patthy, L.,Otting, G. NMR structure of the LCCL domain and implications for DFNA9 deafness disorder. EMBO J., 20:5347-5353, 2001 Cited by PubMed Abstract: The LCCL domain is a recently discovered, conserved protein module named after its presence in Limulus factor C, cochlear protein Coch-5b2 and late gestation lung protein Lgl1. The LCCL domain plays a key role in the autosomal dominant human deafness disorder DFNA9. Here we report the nuclear magnetic resonance (NMR) structure of the LCCL domain from human Coch-5b2, where dominant mutations leading to DFNA9 deafness disorder have been identified. The fold is novel. Four of the five known DFNA9 mutations are shown to involve at least partially solvent-exposed residues. Except for the Trp91Arg mutant, expression of these four LCCL mutants resulted in misfolded proteins. These results suggest that Trp91 participates in the interaction with a binding partner. The unexpected sensitivity of the fold with respect to mutations of solvent-accessible residues might be attributed to interference with the folding pathway of this disulfide-containing domain. PubMed: 11574466DOI: 10.1093/emboj/20.19.5347 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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