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Publication Abstract from PubMed

Liprins are a conserved family of scaffolding proteins important for the proper regulation and development of neuronal synapses. Humans have four liprin-alphas and two liprin-betas which all contain long coiled-coil domains followed by three tandem SAM domains. Complex interactions between the coiled-coil and SAM domains are thought to create liprin scaffolds, but the structural and biochemical properties of these domains remain largely uncharacterized. In this study we find that the human liprin-beta2 coiled-coil forms an extended dimer. Several protease-resistant subdomains within the liprin-beta1 and liprin-beta2 coiled-coils were also identified. A 2.0 A crystal structure of the central, protease-resistant core of the liprin-beta2 coiled-coil reveals a parallel helix orientation. These studies represent an initial step toward determining the overall architecture of liprin scaffolds and understanding the molecular basis for their synaptic functions.

Crystal structure of the central coiled-coil domain from human liprin-beta2.,Stafford RL, Tang MY, Sawaya MR, Phillips ML, Bowie JU Biochemistry. 2011 May 10;50(18):3807-15. Epub 2011 Apr 15. PMID:21462929^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.