1EGG

STRUCTURE OF A C-TYPE CARBOHYDRATE-RECOGNITION DOMAIN (CRD-4) FROM THE MACROPHAGE MANNOSE RECEPTOR

1EGG の概要

• エントリーDOI: 10.2210/pdb1egg/pdb
• 関連するPDBエントリー: 1EGI
• 分子名称: MACROPHAGE MANNOSE RECEPTOR, CALCIUM ION (3 entities in total)
• 機能のキーワード: c-type lectin, mannose receptor, sugar binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Endosome membrane; Single-pass type I membrane protein: P22897
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33721.43

構造登録者

Feinberg, H.,Park-Snyder, S.,Kolatkar, A.R.,Heise, C.T.,Taylor, M.E.,Weis, W.I. (登録日: 2000-02-15, 公開日: 2000-08-30, 最終更新日: 2024-10-30)

主引用文献

Feinberg, H.,Park-Snyder, S.,Kolatkar, A.R.,Heise, C.T.,Taylor, M.E.,Weis, W.I.
Structure of a C-type carbohydrate recognition domain from the macrophage mannose receptor.
J.Biol.Chem., 275:21539-21548, 2000

PubMed Abstract: The mannose receptor of macrophages and liver endothelium mediates clearance of pathogenic organisms and potentially harmful glycoconjugates. The extracellular portion of the receptor includes eight C-type carbohydrate recognition domains (CRDs), of which one, CRD-4, shows detectable binding to monosaccharide ligands. We have determined the crystal structure of CRD-4. Although the basic C-type lectin fold is preserved, a loop extends away from the core of the domain to form a domain-swapped dimer in the crystal. Of the two Ca(2+) sites, only the principal site known to mediate carbohydrate binding in other C-type lectins is occupied. This site is altered in a way that makes sugar binding impossible in the mode observed in other C-type lectins. The structure is likely to represent an endosomal form of the domain formed when Ca(2+) is lost from the auxiliary calcium site. The structure suggests a mechanism for endosomal ligand release in which the auxiliary calcium site serves as a pH sensor. Acid pH-induced removal of this Ca(2+) results in conformational rearrangements of the receptor, rendering it unable to bind carbohydrate ligands.

PubMed: 10779515
DOI: 10.1074/jbc.M002366200

実験手法

X-RAY DIFFRACTION (2.3 Å)