Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1KZD

Complex of MBP-C and GlcNAc-terminated core

1KZD の概要
エントリーDOI10.2210/pdb1kzd/pdb
関連するPDBエントリー1KZA 1KZB 1KZC 1KZE 1RDO
分子名称MANNOSE-BINDING PROTEIN C, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
機能のキーワードprotein-carbohydrate complex, immune system, sugar binding protein
由来する生物種Rattus norvegicus (Norway rat)
タンパク質・核酸の鎖数2
化学式量合計26263.38
構造登録者
Ng, K.K.,Kolatkar, A.R.,Park-Snyder, S.,Feinberg, H.,Clark, D.A.,Drickamer, K.,Weis, W.I. (登録日: 2002-02-06, 公開日: 2002-07-05, 最終更新日: 2024-10-09)
主引用文献Ng, K.K.,Kolatkar, A.R.,Park-Snyder, S.,Feinberg, H.,Clark, D.A.,Drickamer, K.,Weis, W.I.
Orientation of bound ligands in mannose-binding proteins. Implications for multivalent ligand recognition.
J.Biol.Chem., 277:16088-16095, 2002
Cited by
PubMed Abstract: Mannose-binding proteins (MBPs) are C-type animal lectins that recognize high mannose oligosaccharides on pathogenic cell surfaces. MBPs bind to their carbohydrate ligands by forming a series of Ca(2+) coordination and hydrogen bonds with two hydroxyl groups equivalent to the 3- and 4-OH of mannose. In this work, the determinants of the orientation of sugars bound to rat serum and liver MBPs (MBP-A and MBP-C) have been systematically investigated. The crystal structures of MBP-A soaked with monosaccharides and disaccharides and also the structure of the MBP-A trimer cross-linked by a high mannose asparaginyl oligosaccharide reveal that monosaccharides or alpha1-6-linked mannose bind to MBP-A in one orientation, whereas alpha1-2- or alpha1-3-linked mannose binds in an orientation rotated 180 degrees around a local symmetry axis relating the 3- and 4-OH groups. In contrast, a similar set of ligands all bind to MBP-C in a single orientation. The mutation of MBP-A His(189) to its MBP-C equivalent, valine, causes Man alpha 1-3Man to bind in a mixture of orientations. These data combined with modeling indicate that the residue at this position influences the orientation of bound ligands in MBP. We propose that the control of binding orientation can influence the recognition of multivalent ligands. A lateral association of trimers in the cross-linked crystals may reflect interactions within higher oligomers of MBP-A that are stabilized by multivalent ligands.
PubMed: 11850428
DOI: 10.1074/jbc.M200493200
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.9 Å)
構造検証レポート
Validation report summary of 1kzd
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

PDB statisticsPDBj update infoContact PDBjnumon