4QPY

Crystal structure of C1QL2

4QPY の概要

• エントリーDOI: 10.2210/pdb4qpy/pdb
• 関連するPDBエントリー: 4qq2 4qqh 4qql 4qqo 4qqp
• 分子名称: Complement C1q-like protein 2 (2 entities in total)
• 機能のキーワード: jelly roll fold, brain-specific angiogenesis inhibitor adhesion g-protein coupled receptor 3, extracellular, protein binding
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Secreted : Q8CFR0
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 44809.51

構造登録者

Ressl, S.,Brunger, A.T. (登録日: 2014-06-25, 公開日: 2015-04-15, 最終更新日: 2024-02-28)

主引用文献

Ressl, S.,Vu, B.K.,Vivona, S.,Martinelli, D.C.,Sudhof, T.C.,Brunger, A.T.
Structures of C1q-like Proteins Reveal Unique Features among the C1q/TNF Superfamily.
Structure, 23:688-699, 2015

PubMed Abstract: C1q-like (C1QL) -1, -2, and -3 proteins are encoded by homologous genes that are highly expressed in brain. C1QLs bind to brain-specific angiogenesis inhibitor 3 (BAI3), an adhesion-type G-protein coupled receptor that may regulate dendritic morphology by organizing actin filaments. To begin to understand the function of C1QLs, we determined high-resolution crystal structures of the globular C1q-domains of C1QL1, C1QL2, and C1QL3. Each structure is a trimer, with each protomer forming a jelly-roll fold consisting of 10 β strands. Moreover, C1QL trimers may assemble into higher-order oligomers similar to adiponectin and contain four Ca(2+)-binding sites along the trimeric symmetry axis, as well as additional surface Ca(2+)-binding sites. Mutation of Ca(2+)-coordinating residues along the trimeric symmetry axis lowered the Ca(2+)-binding affinity and protein stability. Our results reveal unique structural features of C1QLs among C1q/TNF superfamily proteins that may be associated with their specific brain functions.

PubMed: 25752542
DOI: 10.1016/j.str.2015.01.019

実験手法

X-RAY DIFFRACTION (2.384 Å)