5ng4
Human CEP135 parallel dimeric coiled coil 82-144
Structural highlights
DiseaseCP135_HUMAN Autosomal recessive primary microcephaly. The disease is caused by mutations affecting the gene represented in this entry. FunctionCP135_HUMAN Centrosomal protein involved in centriole biogenesis. Acts as a scaffolding protein during early centriole biogenesis. Required for the targeting of centriole satellite proteins to centrosomes such as of PCM1, SSX2IP and CEP290 and recruitment of WRAP73 to centrioles. Also required for centriole-centriole cohesion during interphase by acting as a platform protein for CEP250 at the centriole.[1] [2] [3] Publication Abstract from PubMedCoiled 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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