6SA4

SALSA / DMBT1 / GP340 SRCR domain 1

6SA4 の概要

• エントリーDOI: 10.2210/pdb6sa4/pdb
• 分子名称: Deleted in malignant brain tumors 1 protein, MAGNESIUM ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: scavenger receptor cysteine-rich, pattern recognition, mucosal immunology, anti-microbial molecule, complement, innate immunity, inflammation, salivary agglutinin, salivary scavenger and agglutinin, immune system
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15793.27

構造登録者

Reichhardt, M.P.,Lea, S.M.,Johnson, S. (登録日: 2019-07-16, 公開日: 2020-03-18, 最終更新日: 2024-11-13)

主引用文献

Reichhardt, M.P.,Loimaranta, V.,Lea, S.M.,Johnson, S.
Structures of SALSA/DMBT1 SRCR domains reveal the conserved ligand-binding mechanism of the ancient SRCR fold.
Life Sci Alliance, 3:-, 2020

PubMed Abstract: The scavenger receptor cysteine-rich (SRCR) family of proteins comprises more than 20 membrane-associated and secreted molecules. Characterised by the presence of one or more copies of the ∼110 amino-acid SRCR domain, this class of proteins have widespread functions as antimicrobial molecules, scavenger receptors, and signalling receptors. Despite the high level of structural conservation of SRCR domains, no unifying mechanism for ligand interaction has been described. The SRCR protein SALSA, also known as DMBT1/gp340, is a key player in mucosal immunology. Based on detailed structural data of SALSA SRCR domains 1 and 8, we here reveal a novel universal ligand-binding mechanism for SALSA ligands. The binding interface incorporates a dual cation-binding site, which is highly conserved across the SRCR superfamily. Along with the well-described cation dependency on most SRCR domain-ligand interactions, our data suggest that the binding mechanism described for the SALSA SRCR domains is applicable to all SRCR domains. We thus propose to have identified in SALSA a conserved functional mechanism for the SRCR class of proteins.

PubMed: 32098784
DOI: 10.26508/lsa.201900502

実験手法

X-RAY DIFFRACTION (1.77 Å)