Abstract
The synaptonemal complex protein 1 (SYCP1) is the main structural element of transverse filaments (TFs) of the synaptonemal complex (SC), which is a meiosis-specific complex structure formed at the synapse of homologue chromosomes to hold them together. The N-terminal domain of SYCP1 is known to be located within the central elements (CEs), whereas the C-terminal domain is located toward lateral elements (LEs). SYCP1 is a well-known meiosis marker that is also known to be a prognostic marker in the early stage of several cancers including breast, gliomas, and ovarian cancers. The structure of SC, especially the TF structure formed mainly by SYCP1, remains unclear without any structural information. To elucidate a molecular basis of SC formation and function, we first solved the crystal structure of C-terminal coiled-coil domain of SYCP1. The coiled-coil domain of SYCP1 forms asymmetric, anti-parallel dimers in solution.
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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Cloning, Molecular
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Conserved Sequence
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Crystallography, X-Ray
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DNA-Binding Proteins
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Gene Expression
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Humans
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Meiosis
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Models, Molecular
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Nuclear Proteins / chemistry*
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism
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Protein Binding
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Protein Interaction Domains and Motifs
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Protein Multimerization
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Protein Structure, Secondary
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Sequence Alignment
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Sequence Homology, Amino Acid
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Synaptonemal Complex / genetics
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Synaptonemal Complex / metabolism
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Synaptonemal Complex / ultrastructure*
Substances
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DNA-Binding Proteins
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Nuclear Proteins
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Recombinant Proteins
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SYCP1 protein, human
Grants and funding
This study was supported by the Korea Healthcare Technology Research & Development project, Ministry of Health & Welfare, Republic of Korea (HI13C1449). This study was supported by Yeungnam University research grants in 2014.