Members of this family adopt a structure consisting of several large open beta-sheets. Their exact function has not, as yet, been determined [(PUBMED:12135361)].
Family alignment:
There are 95
DUF1944 domains in 95 proteins in SMART's nrdb database.
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Evolution (species in which this domain is found)
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This tree shows only several representative species. The complete taxonomic breakdown of all proteins with DUF1944 domain is also avaliable.
The refined molecular structure of lipovitellin is described using synchrotroncryocrystallographic data to 1.9 A resolution. Lipovitellin is the predominantlipoprotein found in the yolk of egg-laying animals and is involved in lipid and metal storage. It is thought to be related in amino acid sequence to segments of apolipoprotein B and the microsomal transfer protein responsible for the assemblyof low-density lipoproteins. Lipovitellin contains a heterogeneous mixture ofabout 16% (w/w) noncovalently bound lipid, mostly phospholipid. Previous X-raystructural studies at ambient temperature described several different proteindomains including a large cavity in each subunit of the dimeric protein. Thecavity was free of any visible electron density for lipid molecules at roomtemperature, suggesting that only dynamic interactions exist with the protein. Animportant result from this crystallographic study at 100 K is the appearance ofsome bound ordered lipid along the walls of the binding cavity. The preciseidentification of the lipid type is difficult because of discontinuities in theelectron density. Nonetheless, the conformations of 7 phospholipids and 43segments of hydrocarbon chains greater than 5 atoms in length have beendiscovered. The conformations of the bound lipid and the interactions betweenprotein and lipid provide insights into the factors governing lipoproteinformation.
to expand nodes. To display all proteins with a DUF1944 domain in a specific node, click on it.