1BV4

APO-MANNOSE-BINDING PROTEIN-C

1BV4 の概要

• エントリーDOI: 10.2210/pdb1bv4/pdb
• 分子名称: PROTEIN (MANNOSE-BINDING PROTEIN-C) (2 entities in total)
• 機能のキーワード: c-type lectin, calcium-binding protein, collectin, sugar binding protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 52646.42

構造登録者

Ng, K.K.-S.,Weis, W.I. (登録日: 1998-09-22, 公開日: 1999-01-13, 最終更新日: 2024-10-30)

主引用文献

Ng, K.K.,Park-Snyder, S.,Weis, W.I.
Ca2+-dependent structural changes in C-type mannose-binding proteins.
Biochemistry, 37:17965-17976, 1998

PubMed Abstract: C-type animal lectins are a diverse family of proteins which mediate cell-surface carbohydrate-recognition events through a conserved carbohydrate-recognition domain (CRD). Most members of this family possess a carbohydrate-binding activity that depends strictly on the binding of Ca2+ at two sites, designated 1 and 2, in the CRD. The structural transitions associated with Ca2+ binding in C-type lectins have been investigated by determining high-resolution crystal structures of rat serum mannose-binding protein (MBP) bound to one Ho3+ in place of Ca2+, and the apo form of rat liver MBP. The removal of Ca2+ does not affect the core structure of the CRD, but dramatic conformational changes occur in the loops. The most significant structural change in the absence of Ca2+ is the isomerization of a cis-peptide bond preceding a conserved proline residue in Ca2+ site 2. This bond adopts the cis conformation in all Ca2+-bound structures, whereas both cis and trans conformations are observed in the absence of Ca2+. The pattern of structural changes in the three loops that interact with Ca2+ is dictated in large part by the conformation of the prolyl peptide bond. The highly conserved nature of Ca2+ site 2 suggests that the transitions observed in MBPs are general features of Ca2+ binding in C-type lectins.

PubMed: 9922165
DOI: 10.1021/bi981972a

実験手法

X-RAY DIFFRACTION (1.85 Å)