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Crystallization and preliminary X-ray diffraction studies of an RNA aptamer in complex with the human IgG Fc fragment.

ABSTRACT: 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 A. A data set has been collected to 2.2 A resolution.

SUBMITTER: Sugiyama S 

PROVIDER: S-EPMC2564881 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction studies of an RNA aptamer in complex with the human IgG Fc fragment.

Sugiyama Shigeru S   Nomura Yusuke Y   Sakamoto Taiichi T   Kitatani Tomoya T   Kobayashi Asako A   Miyakawa Shin S   Takahashi Yoshinori Y   Adachi Hiroaki H   Takano Kazufumi K   Murakami Satoshi S   Inoue Tsuyoshi T   Mori Yusuke Y   Nakamura Yoshikazu Y   Matsumura Hiroyoshi H  

Acta crystallographica. Section F, Structural biology and crystallization communications 20080930 Pt 10

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 Ig  ...[more]

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