1XAR

Crystal Structure of a fragment of DC-SIGNR (containing the carbohydrate recognition domain and two repeats of the neck).

1XAR の概要

• エントリーDOI: 10.2210/pdb1xar/pdb
• 分子名称: CD209 antigen-like protein 1, SODIUM ION (3 entities in total)
• 機能のキーワード: dc-signr, c-type lectin, sugar binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Isoform 1: Cell membrane; Single-pass type II membrane protein (Potential). Isoform 2: Cell membrane; Single-pass type II membrane protein (Potential). Isoform 3: Cell membrane; Single-pass type II membrane protein (Potential). Isoform 5: Secreted (Potential). Isoform 6: Secreted (Potential). Isoform 7: Secreted (Potential). Isoform 10: Secreted (Potential): Q9H2X3
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42900.97

構造登録者

Feinberg, H.,Guo, Y.,Mitchell, D.A.,Drickamer, K.,Weis, W.I. (登録日: 2004-08-26, 公開日: 2004-11-16, 最終更新日: 2024-11-20)

主引用文献

Feinberg, H.,Guo, Y.,Mitchell, D.A.,Drickamer, K.,Weis, W.I.
Extended Neck Regions Stabilize Tetramers of the Receptors DC-SIGN and DC-SIGNR
J.Biol.Chem., 280:1327-1335, 2005

PubMed Abstract: The human cell surface receptors DC-SIGN (dendritic cell-specific intercellular adhesion molecule-grabbing nonintegrin) and DC-SIGNR (DC-SIGN-related) bind to oligosaccharide ligands found on human tissues as well as on pathogens including viruses, bacteria, and parasites. The extracellular portion of each receptor contains a membrane-distal carbohydrate-recognition domain (CRD) and forms tetramers stabilized by an extended neck region consisting of 23 amino acid repeats. Cross-linking analysis of full-length receptors expressed in fibroblasts confirms the tetrameric state of the intact receptors. Hydrodynamic studies on truncated receptors demonstrate that the portion of the neck of each protein adjacent to the CRD is sufficient to mediate the formation of dimers, whereas regions near the N terminus are needed to stabilize the tetramers. Some of the intervening repeats are missing from polymorphic forms of DC-SIGNR. Two different crystal forms of truncated DC-SIGNR comprising two neck repeats and the CRD reveal that the CRDs are flexibly linked to the neck, which contains alpha-helical segments interspersed with non-helical regions. Differential scanning calorimetry measurements indicate that the neck and CRDs are independently folded domains. Based on the crystal structures and hydrodynamic data, models for the full extracellular domains of the receptors have been generated. The observed flexibility of the CRDs in the tetramer, combined with previous data on the specificity of these receptors, suggests an important role for oligomerization in the recognition of endogenous glycans, in particular those present on the surfaces of enveloped viruses recognized by these proteins.

PubMed: 15509576
DOI: 10.1074/jbc.M409925200

実験手法

X-RAY DIFFRACTION (2.25 Å)