1C28
THE CRYSTAL STRUCTURE OF A COMPLMENT-1Q FAMILY PROTEIN SUGGESTS AN EVOLUTIONARY LINK TO TUMOR NECROSIS FACTOR
1C28 の概要
| エントリーDOI | 10.2210/pdb1c28/pdb |
| 分子名称 | PROTEIN (30 KD ADIPOCYTE COMPLEMENT-RELATED PROTEIN PRECURSOR (ACRP30)) (2 entities in total) |
| 機能のキーワード | acrp30 c1q tnf trimer all-beta, serum protein |
| 由来する生物種 | Mus musculus (house mouse) |
| 細胞内の位置 | Secreted: Q60994 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 46879.21 |
| 構造登録者 | |
| 主引用文献 | Shapiro, L.,Scherer, P.E. The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor. Curr.Biol., 8:335-338, 1998 Cited by PubMed Abstract: ACRP30--adipocyte complement-related protein of 30 kDa or AdipoQ--is an abundant serum protein, secreted exclusively from fat cells, which is implicated in energy homeostasis and obesity [1,2]. ACRP30 is a close homologue of the complement protein C1q, which is involved in the recognition of microbial surfaces [3-5] and antibody-antigen complexes [6,7] in the classical pathway of complement. We have determined the crystal structure of a homotrimeric fragment from ACRP30 at 2.1 A resolution. The structure reveals an unexpected homology to the tumor necrosis factor (TNF) family. Identical folding topologies, key residue conservations, and similarity of trimer interfaces and intron positions firmly establish an evolutionary link between the TNF and C1q families. We suggest that TNFs--which control many aspects of inflammation, adaptive immunity, apoptosis and energy homeostasis--arose by divergence from a primordial recognition molecule of the innate immune system. The evolutionary connection between C1q-like proteins and TNFs illuminates the shared functions of these two important groups of proteins. PubMed: 9512423DOI: 10.1016/S0960-9822(98)70133-2 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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