+
データを開く
-
基本情報
登録情報 | データベース: PDB / ID: 8t4f | ||||||
---|---|---|---|---|---|---|---|
タイトル | Transporter associated with antigen processing (TAP) bound to the 9-mer peptide RRYQKSTEL | ||||||
![]() |
| ||||||
![]() | MEMBRANE PROTEIN / ABC transporter / antigen processing / peptide transporter | ||||||
機能・相同性 | ![]() antigen processing and presentation of endogenous peptide antigen via MHC class Ib via ER pathway, TAP-dependent / tapasin binding / ABC-type peptide antigen transporter activity / ABC-type antigen peptide transporter / TAP complex / ABC-type peptide transporter activity / TAP2 binding / TAP1 binding / MHC class Ib protein binding / peptide antigen transport ...antigen processing and presentation of endogenous peptide antigen via MHC class Ib via ER pathway, TAP-dependent / tapasin binding / ABC-type peptide antigen transporter activity / ABC-type antigen peptide transporter / TAP complex / ABC-type peptide transporter activity / TAP2 binding / TAP1 binding / MHC class Ib protein binding / peptide antigen transport / cytosol to endoplasmic reticulum transport / peptide transport / peptide transmembrane transporter activity / nucleosomal DNA binding / MHC class I protein binding / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent / endoplasmic reticulum-Golgi intermediate compartment membrane / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / response to molecule of bacterial origin / MHC class I peptide loading complex / euchromatin / defense response / T cell mediated cytotoxicity / ADP binding / antigen processing and presentation of endogenous peptide antigen via MHC class I / peptide antigen binding / positive regulation of T cell mediated cytotoxicity / transmembrane transport / centriolar satellite / phagocytic vesicle membrane / structural constituent of chromatin / nucleosome / protein transport / ER-Phagosome pathway / positive regulation of cell growth / adaptive immune response / nuclear speck / protein heterodimerization activity / endoplasmic reticulum membrane / endoplasmic reticulum / protein homodimerization activity / ATP hydrolysis activity / nucleoplasm / ATP binding / metal ion binding / nucleus / membrane 類似検索 - 分子機能 | ||||||
生物種 | ![]() | ||||||
手法 | 電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 3.5 Å | ||||||
![]() | Lee, J. / Oldham, M.L. / Chen, J. | ||||||
資金援助 | ![]()
| ||||||
![]() | ![]() タイトル: Principles of peptide selection by the transporter associated with antigen processing. 著者: James Lee / Michael L Oldham / Victor Manon / Jue Chen / ![]() 要旨: Our ability to fight pathogens relies on major histocompatibility complex class I (MHC-I) molecules presenting diverse antigens on the surface of diseased cells. The transporter associated with ...Our ability to fight pathogens relies on major histocompatibility complex class I (MHC-I) molecules presenting diverse antigens on the surface of diseased cells. The transporter associated with antigen processing (TAP) transports nearly the entire repertoire of antigenic peptides into the endoplasmic reticulum for MHC-I loading. How TAP transports peptides specific for MHC-I is unclear. In this study, we used cryo-EM to determine a series of structures of human TAP, both in the absence and presence of peptides with various sequences and lengths. The structures revealed that peptides of eight or nine residues in length bind in a similarly extended conformation, despite having little sequence overlap. We also identified two peptide-anchoring pockets on either side of the transmembrane cavity, each engaging one end of a peptide with primarily main chain atoms. Occupation of both pockets results in a global conformational change in TAP, bringing the two halves of the transporter closer together to prime it for isomerization and ATP hydrolysis. Shorter peptides are able to bind to each pocket separately but are not long enough to bridge the cavity to bind to both simultaneously. Mutations that disrupt hydrogen bonds with the N and C termini of peptides almost abolish MHC-I surface expression. Our findings reveal that TAP functions as a molecular caliper that selects peptides according to length rather than sequence, providing antigen diversity for MHC-I presentation. | ||||||
履歴 |
|
-
構造の表示
構造ビューア | 分子: ![]() ![]() |
---|
-
ダウンロードとリンク
-
ダウンロード
PDBx/mmCIF形式 | ![]() | 197.9 KB | 表示 | ![]() |
---|---|---|---|---|
PDB形式 | ![]() | 146.7 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
文書・要旨 | ![]() | 1.5 MB | 表示 | ![]() |
---|---|---|---|---|
文書・詳細版 | ![]() | 1.5 MB | 表示 | |
XML形式データ | ![]() | 49.1 KB | 表示 | |
CIF形式データ | ![]() | 72.6 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
関連構造データ | ![]() 41029MC ![]() 8t46C ![]() 8t4eC ![]() 8t4gC ![]() 8t4hC ![]() 8t4iC ![]() 8t4jC M: このデータのモデリングに利用したマップデータ C: 同じ文献を引用 ( |
---|---|
類似構造データ | 類似検索 - 機能・相同性 ![]() |
-
リンク
-
集合体
登録構造単位 | ![]()
|
---|---|
1 |
|
-
要素
#1: タンパク質 | 分子量: 81034.289 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
---|---|
#2: タンパク質 | 分子量: 75736.508 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
#3: タンパク質・ペプチド | 分子量: 1183.338 Da / 分子数: 1 / 由来タイプ: 合成 / 由来: (合成) ![]() |
Has protein modification | N |
-実験情報
-実験
実験 | 手法: 電子顕微鏡法 |
---|---|
EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: 単粒子再構成法 |
-
試料調製
構成要素 | 名称: Transporter associated with antigen processing bound to the 9-mer peptide RRYQKSTEL タイプ: COMPLEX / 詳細: Complex of TAP1 and TAP2 / Entity ID: all / 由来: MULTIPLE SOURCES | |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
分子量 | 値: 0.156 MDa / 実験値: YES | |||||||||||||||||||||||||
由来(天然) | 生物種: ![]() | |||||||||||||||||||||||||
由来(組換発現) | 生物種: ![]() | |||||||||||||||||||||||||
緩衝液 | pH: 6.5 | |||||||||||||||||||||||||
緩衝液成分 |
| |||||||||||||||||||||||||
試料 | 濃度: 6 mg/ml / 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES | |||||||||||||||||||||||||
試料支持 | グリッドの材料: GOLD / グリッドのサイズ: 400 divisions/in. / グリッドのタイプ: Quantifoil R1.2/1.3 | |||||||||||||||||||||||||
急速凍結 | 装置: FEI VITROBOT MARK IV / 凍結剤: ETHANE / 湿度: 100 % / 凍結前の試料温度: 279 K |
-
電子顕微鏡撮影
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
---|---|
顕微鏡 | モデル: FEI TITAN KRIOS |
電子銃 | 電子線源: ![]() |
電子レンズ | モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 2500 nm / 最小 デフォーカス(公称値): 800 nm / アライメント法: COMA FREE |
試料ホルダ | 凍結剤: NITROGEN 試料ホルダーモデル: FEI TITAN KRIOS AUTOGRID HOLDER |
撮影 | 電子線照射量: 66 e/Å2 / フィルム・検出器のモデル: GATAN K3 (6k x 4k) |
-
解析
EMソフトウェア |
| ||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||
粒子像の選択 | 選択した粒子像数: 1618719 | ||||||||||||||||||||||||||||
3次元再構成 | 解像度: 3.5 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 73744 / 対称性のタイプ: POINT | ||||||||||||||||||||||||||||
精密化 | 交差検証法: NONE |