Crystal structure of human transgelin |
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Authors: | Li Ming Li Shentao Lou Zhiyong Liao Xiaoping Zhao Xiaodong Meng Zhaohui Bartlam Mark Rao Zihe |
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Affiliation: | "Tsinghua-Nankai-IBP Joint Research Group for Structural Biology", Tsinghua University, Beijing 100084, China. |
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Abstract: | Transgelin (TAGLN), also known as smooth muscle protein 22 (SM22), is a highly conserved protein found in smooth muscle tissues of adult vertebrates. Abolition of transgelin gene expression by the oncogenic Ras may be an important early event in tumor progression and a diagnostic marker for breast and colon cancer development. Transgelin contains a single calponin homology (CH) domain. However, the question of whether this single CH domain can bind actin remains open. Here we report the 2.3 A resolution crystal structure of full length human transgelin, whose main structural feature is confirmed to be a CH domain. Secondary structures of CH domains from different proteins were analyzed and conserved residues were identified that maintain similar tertiary structures. |
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