Human phosphatidylcholine transfer protein: purification, crystallization and preliminary X-ray diffraction data.

Article Details

Citation

Chan WW, Roderick SL, Cohen DE

Human phosphatidylcholine transfer protein: purification, crystallization and preliminary X-ray diffraction data.

Biochim Biophys Acta. 2002 Apr 1;1596(1):1-5.

PubMed ID
11983415 [ View in PubMed
]
Abstract

We have expressed, purified and crystallized recombinant human phosphatidylcholine transfer protein (PC-TP) and selenomethionyl PC-TP bound to dilinoleoyl phosphatidylcholine. The biochemical properties of native and selenomethionyl PC-TP were indistinguishable, and the two proteins crystallized under similar conditions. Both native and selenomethionyl PC-TP crystallized in two distinct space groups and diffracted X-rays to 2.4 A resolution.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Phosphatidylcholine transfer proteinQ9UKL6Details