4FQP

Crystal structure of human Nectin-like 5 full ectodomain (D1-D3)

4FQP の概要

• エントリーDOI: 10.2210/pdb4fqp/pdb
• 関連するPDBエントリー: 4FMF 4FMK 4FN0 4FOM 4FRW 4FS0
• 分子名称: Poliovirus receptor, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: immunoglobulin-like domain, ig domain, viral entry receptor, cell adhesion
• 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: 38137.20

構造登録者

Harrison, O.J.,Jin, X.,Brasch, J.,Shapiro, L. (登録日: 2012-06-25, 公開日: 2012-08-22, 最終更新日: 2024-11-20)

主引用文献

Harrison, O.J.,Vendome, J.,Brasch, J.,Jin, X.,Hong, S.,Katsamba, P.S.,Ahlsen, G.,Troyanovsky, R.B.,Troyanovsky, S.M.,Honig, B.,Shapiro, L.
Nectin ectodomain structures reveal a canonical adhesive interface.
Nat.Struct.Mol.Biol., 19:906-915, 2012

PubMed Abstract: Nectins are immunoglobulin superfamily glycoproteins that mediate intercellular adhesion in many vertebrate tissues. Homophilic and heterophilic interactions between nectin family members help mediate tissue patterning. We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern. To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5. All of the crystal structures revealed dimeric nectins bound through a stereotyped interface that was previously proposed to represent a cis dimer. However, conservation of this interface and the results of targeted cross-linking experiments showed that this dimer probably represents the adhesive trans interaction. The structure of the dimer provides a simple molecular explanation for the adhesive binding specificity of nectins.

PubMed: 22902367
DOI: 10.1038/nsmb.2366

実験手法

X-RAY DIFFRACTION (3.6 Å)