2ZV6
Crystal structure of human squamous cell carcinoma antigen 1
Summary for 2ZV6
Entry DOI | 10.2210/pdb2zv6/pdb |
Descriptor | Serpin B3 (2 entities in total) |
Functional Keywords | serine proteinase inhibitor, reactive site loop, acetylation, alternative splicing, cytoplasm, polymorphism, protease inhibitor, serine protease inhibitor, hydrolase inhibitor |
Biological source | Homo sapiens (Human) |
Cellular location | Cytoplasm: P29508 |
Total number of polymer chains | 3 |
Total formula weight | 137684.36 |
Authors | Zheng, B.,Matoba, Y.,Katagiri, C.,Hibino, T.,Sugiyama, M. (deposition date: 2008-11-01, release date: 2009-02-24, Last modification date: 2023-11-01) |
Primary citation | Zheng, B.,Matoba, Y.,Kumagai, T.,Katagiri, C.,Hibino, T.,Sugiyama, M. Crystal structure of SCCA1 and insight about the interaction with JNK1 Biochem.Biophys.Res.Commun., 380:143-147, 2009 Cited by PubMed Abstract: Squamous cell carcinoma antigen 1 (SCCA1), which belongs to serine proteinase inhibitor (serpin) superfamily, inhibits papain-like cysteine proteinase. Recently, it has been reported that SCCA1 acts not only as a proteinase inhibitor but also as an inhibitor of UV-induced apoptosis via suppression of the activity of c-Jun NH(2)-terminal kinase (JNK1). The present study determined the crystal structure of SCCA1, suggesting that the reactive center loop (RCL) of SCCA1, a recognition site of proteinase, is very flexible and located away form the main-body of SCCA1. We show that the inhibitory effect of SCCA1 on the kinase activity of JNK1 is lost when the RCL was truncated. Furthermore, we found that a mutant protein created by replacing one amino acid in RCL maintain the suppressive activity to JNK1, whereas the inhibitory effect to proteinase is obviously decreased. PubMed: 19166818DOI: 10.1016/j.bbrc.2009.01.057 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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