Structural highlights
Disease
[KI21A_HUMAN] Congenital fibrosis of extraocular muscles. The disease is caused by mutations affecting the gene represented in this entry.
Function
[KI21A_HUMAN] Microtubule-binding motor protein probably involved in neuronal axonal transport. In vitro, has a plus-end directed motor activity (By similarity).
Publication Abstract from PubMed
Coiled coils are ubiquitous protein-protein interaction motifs found in many eukaryotic proteins. The elongated, flexible and often irregular natureof coiled coils together with their tendency to form fibrous arrangements in crystals impose challenges on solving the phase problem by molecular replacement. Here, we report the successful combinatorial use of native- and rational engineered disulfide bridges together with sulfur-SAD phasing as a powerful tool to stabilize and solve the structure of coiled-coil domains in a straightforward manner. Our study is a key example of how modern sulfur SAD combined with mutagenesis can help to advance and simplify the structural study of challenging coiled-coil domains by X-ray crystallography.
Combinatorial use of disulfide bridges and native sulfur-SAD phasing for rapid structure determination of coiled-coils.,Kraatz SHW, Bianchi S, Steinmetz MO Biosci Rep. 2018 Aug 22. pii: BSR20181073. doi: 10.1042/BSR20181073. PMID:30135143[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kraatz SHW, Bianchi S, Steinmetz MO. Combinatorial use of disulfide bridges and native sulfur-SAD phasing for rapid structure determination of coiled-coils. Biosci Rep. 2018 Aug 22. pii: BSR20181073. doi: 10.1042/BSR20181073. PMID:30135143 doi:http://dx.doi.org/10.1042/BSR20181073
