2KNY

Fusion construct of CR17 from LRP-1 and ApoE residues 130-149

2KNY の概要

• エントリーDOI: 10.2210/pdb2kny/pdb
• NMR情報: BMRB: 16483
• 分子名称: LRP-1, linker, Apo-E, CALCIUM ION (2 entities in total)
• 機能のキーワード: lrp, apoe, lipoprotein receptor, ligand binding module, complement repeat, calcium, cell membrane, coated pit, cytoplasm, developmental protein, disulfide bond, egf-like domain, endocytosis, glycoprotein, membrane, metal-binding, nucleus, phosphoprotein, polymorphism, receptor, transmembrane, protein binding, metal binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8439.51

構造登録者

Guttman, M.,Komives, E.A. (登録日: 2009-09-08, 公開日: 2010-04-14, 最終更新日: 2024-10-30)

主引用文献

Guttman, M.,Prieto, J.H.,Handel, T.M.,Domaille, P.J.,Komives, E.A.
Structure of the minimal interface between ApoE and LRP.
J.Mol.Biol., 398:306-319, 2010

PubMed Abstract: Clusters of complement-type ligand-binding repeats (CRs) in the low-density lipoprotein receptor (LDLR) family are thought to mediate the interactions with their various ligands. Apolipoprotein E (ApoE), a key ligand for cholesterol homeostasis, has been shown to interact with LDLR-related protein 1 (LRP) through these clusters. The segment comprising the receptor-binding portion of ApoE (residues 130-149) has been found to have a weak affinity for isolated CRs. We have fused this region of ApoE to a high-affinity CR from LRP (CR17) for structural elucidation of the complex. The interface reveals a motif that has previously been observed in CR domains with other binding partners, but with several novel features. Comparison to free CR17 reveals that very few structural changes result from this binding event, but significant changes in intrinsic dynamics are observed upon binding. NMR perturbation experiments suggest that this interface may be similar to several other ligand interactions with LDLRs.

PubMed: 20303980
DOI: 10.1016/j.jmb.2010.03.022

実験手法

SOLUTION NMR