期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 64, 期 -, 页码 942-944出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309108028236
关键词
-
资金
- Core Research for Evolution Science and Technology ( CREST)
- Japan Science and Technology Agency
- New Energy and Industrial Technology Development Organization (NEDO) of Japan
Aptamers, which are folded DNA or RNA molecules, bind to target molecules with high affinity and specificity. An RNA aptamer specific for the Fc fragment of human immunoglobulin G (IgG) has recently been identified and it has been demonstrated that an optimized 24-nucleotide RNA aptamer binds to the Fc fragment of human IgG and not to other species. In order to clarify the structural basis of the high specificity of the RNA aptamer, it was crystallized in complex with the Fc fragment of human IgG1. Preliminary X-ray diffraction studies revealed that the crystals belonged to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 83.7, b = 107.2, c = 79.0 angstrom. A data set has been collected to 2.2 angstrom resolution.
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