2L7U

Structure of CEL-PEP-RAGE V domain complex

2L7U の概要

• エントリーDOI: 10.2210/pdb2l7u/pdb
• NMR情報: BMRB: 17378
• 分子名称: Advanced glycosylation end product-specific receptor, Serum albumin peptide (2 entities in total)
• 機能のキーワード: v domain, allergen, cleavage on pair of basic residues, lipid-binding, metal-binding, phosphoprotein, secreted
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted. Isoform 10: Cell membrane ; Single-pass type I membrane protein : Q15109; Secreted: P02769
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 12494.21

構造登録者

Xue, J.,Rai, V.,Schmidt, A.,Frolov, S.,Reverdatto, S.,Singer, D.,Chabierski, S.,Xie, J.,Burz, D.,Shekhtman, A.,Hoffman, R. (登録日: 2010-12-23, 公開日: 2011-05-18, 最終更新日: 2023-11-29)

主引用文献

Xue, J.,Rai, V.,Singer, D.,Chabierski, S.,Xie, J.,Reverdatto, S.,Burz, D.S.,Schmidt, A.M.,Hoffmann, R.,Shekhtman, A.
Advanced glycation end product recognition by the receptor for AGEs.
Structure, 19:722-732, 2011

PubMed Abstract: Nonenzymatic protein glycation results in the formation of advanced glycation end products (AGEs) that are implicated in the pathology of diabetes, chronic inflammation, Alzheimer's disease, and cancer. AGEs mediate their effects primarily through a receptor-dependent pathway in which AGEs bind to a specific cell surface associated receptor, the Receptor for AGEs (RAGE). N(ɛ)-carboxy-methyl-lysine (CML) and N(ɛ)-carboxy-ethyl-lysine (CEL), constitute two of the major AGE structures found in tissue and blood plasma, and are physiological ligands of RAGE. The solution structure of a CEL-containing peptide-RAGE V domain complex reveals that the carboxyethyl moiety fits inside a positively charged cavity of the V domain. Peptide backbone atoms make specific contacts with the V domain. The geometry of the bound CEL peptide is compatible with many CML (CEL)-modified sites found in plasma proteins. The structure explains how such patterned ligands as CML (CEL)-proteins bind to RAGE and contribute to RAGE signaling.

PubMed: 21565706
DOI: 10.1016/j.str.2011.02.013

実験手法

SOLUTION NMR