Crystal structure of the coiled‐coil domain of Drosophila TRIM protein Brat

2019 ◽  
Vol 87 (8) ◽  
pp. 706-710 ◽  
Author(s):  
Chunhua Liu ◽  
Zelin Shan ◽  
Jianqiao Diao ◽  
Wenyu Wen ◽  
Wenning Wang
Keyword(s):  
Crystal Structure ◽  
Coiled Coil ◽  
Trim Protein ◽  
Coiled Coil Domain

scholarly journals Crystal Structure of the Central Coiled-Coil Domain from Human Liprin-β2

Biochemistry ◽  
2011 ◽  
Vol 50 (18) ◽  
pp. 3807-3815 ◽  
Author(s):  
Ryan L. Stafford ◽  
Ming-Yun Tang ◽  
Michael R. Sawaya ◽  
Martin L. Phillips ◽  
James U. Bowie
Keyword(s):  
Crystal Structure ◽  
Coiled Coil ◽  
Coiled Coil Domain

scholarly journals Crystal Structure of a Coiled-Coil Domain from Human ROCK I

PLoS ONE ◽  
2011 ◽  
Vol 6 (3) ◽  
pp. e18080 ◽  
Author(s):  
Daqi Tu ◽  
Yiqun Li ◽  
Hyun Kyu Song ◽  
Angela V. Toms ◽  
Christopher J. Gould ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Coiled Coil ◽  
Coiled Coil Domain

scholarly journals TRIM29 in Cutaneous Squamous Cell Carcinoma

2021 ◽  
Vol 8 ◽  
Author(s):  
Che-Yuan Hsu ◽  
Teruki Yanagi ◽  
Hideyuki Ujiie
Keyword(s):  
Malignant Tumors ◽  
Coiled Coil ◽  
Dna Damage Signaling ◽  
Physiological Processes ◽  
Trim Protein ◽  
Coiled Coil Domain ◽  
Zinc Finger Motifs ◽  
Wide Range ◽  
Trim Proteins

Tripartite motif (TRIM) proteins play important roles in a wide range of cell physiological processes, such as signal transduction, transcriptional regulation, innate immunity, and programmed cell death. TRIM29 protein, encoded by the ATDC gene, belongs to the RING-less group of TRIM protein family members. It consists of four zinc finger motifs in a B-box domain and a coiled-coil domain, and makes use of the B-box domain as E3 ubiquitin ligase in place of the RING. TRIM29 was found to be involved in the formation of homodimers and heterodimers in relation to DNA binding; additional studies have also demonstrated its role in carcinogenesis, DNA damage signaling, and the suppression of radiosensitivity. Recently, we reported that TRIM29 interacts with keratins and FAM83H to regulate keratin distribution. Further, in cutaneous SCC, the expression of TRIM29 is silenced by DNA methylation, leading to the loss of TRIM29 and promotion of keratinocyte migration. This paper reviews the role of TRIM family proteins in malignant tumors, especially the role of TRIM29 in cutaneous SCC.

scholarly journals The crystal structure of mouse LC3B in complex with the FYCO1 LIR reveals the importance of the flanking region of the LIR motif

2017 ◽  
Vol 73 (3) ◽  
pp. 130-137 ◽  
Author(s):  
Shunya Sakurai ◽  
Taisuke Tomita ◽  
Toshiyuki Shimizu ◽  
Umeharu Ohto
Keyword(s):  
Crystal Structure ◽  
Coiled Coil ◽  
Adaptor Protein ◽  
Structural Basis ◽  
Core Sequence ◽  
Coiled Coil Domain ◽  
Flanking Sequences ◽  
Flanking Region ◽  
Membrane Components ◽  
Lir Motif

FYVE and coiled-coil domain-containing protein 1 (FYCO1), a multidomain autophagy adaptor protein, mediates microtubule plus-end-directed autophagosome transport by interacting with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7 and phosphatidylinositol 3-phosphate (PI3P). To establish the structural basis for the recognition of FYCO1 by LC3, the crystal structure of mouse LC3B in complex with the FYCO1 LC3-interacting region (LIR) motif peptide was determined. Structural analysis showed that the flanking sequences N-terminal and C-terminal to the LIR core sequence of FYCO1, as well as the tetrapeptide core sequence, were specifically recognized by LC3B and contributed to the binding. Moreover, comparisons of related structures revealed a conserved mechanism of FYCO1 recognition by different LC3 isoforms among different species.

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