1MSB

STRUCTURE OF THE CALCIUM-DEPENDENT LECTIN DOMAIN FROM A RAT MANNOSE-BINDING PROTEIN DETERMINED BY MAD PHASING

1MSB の概要

• エントリーDOI: 10.2210/pdb1msb/pdb
• 分子名称: MANNOSE-BINDING PROTEIN-A, HOLMIUM ATOM (3 entities in total)
• 機能のキーワード: hepatic lectin
• 由来する生物種: Rattus rattus (black rat)
• 細胞内の位置: Secreted: P19999
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26036.02

構造登録者

Weis, W.I.,Drickamer, K.,Hendrickson, W.A. (登録日: 1991-09-23, 公開日: 1992-01-15, 最終更新日: 2024-10-23)

主引用文献

Weis, W.I.,Kahn, R.,Fourme, R.,Drickamer, K.,Hendrickson, W.A.
Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing.
Science, 254:1608-1615, 1991

PubMed Abstract: Calcium-dependent (C-type) animal lectins participate in many cell surface recognition events mediated by protein-carbohydrate interactions. The C-type lectin family includes cell adhesion molecules, endocytic receptors, and extracellular matrix proteins. Mammalian mannose-binding proteins are C-type lectins that function in antibody-independent host defense against pathogens. The crystal structure of the carbohydrate-recognition domain of a rat mannose-binding protein, determined as the holmium-substituted complex by multiwavelength anomalous dispersion (MAD) phasing, reveals an unusual fold consisting of two distinct regions, one of which contains extensive nonregular secondary structure stabilized by two holmium ions. The structure explains the conservation of 32 residues in all C-type carbohydrate-recognition domains, suggesting that the fold seen here is common to these domains. The strong anomalous scattering observed at the Ho LIII edge demonstrates that traditional heavy atom complexes will be generally amenable to the MAD phasing method.

PubMed: 1721241

実験手法

X-RAY DIFFRACTION (2.3 Å)