Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain |
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Authors: | Li Songlin Finley Jim Liu Zhi-Jie Qiu Shi-Hong Chen Hongli Luan Chi-Hao Carson Mike Tsao Jun Johnson David Lin Guangda Zhao Jun Thomas Willie Nagy Lisa A Sha Bingdong DeLucas Lawrence J Wang Bi-Cheng Luo Ming |
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Affiliation: | Southeast Collaboratory for Structural Genomics, University of Georgia, Athens 30602, USA. |
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Abstract: | Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of the CAP-Gly domain of Caenorhabditis elegans F53F4.3 protein, solved by single wavelength sulfur-anomalous phasing, revealed a novel protein fold containing three beta-sheets. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Residues in the groove are highly conserved as measured from the information content of the aligned sequences. The C-terminal tail of another molecule in the crystal is bound in this groove. |
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