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基本情報
登録情報 | データベース: EMDB / ID: EMD-20816 | |||||||||
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タイトル | Structure of M-6-P/IGFII Receptor and IGFII complex | |||||||||
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機能・相同性 | ![]() kringle domain binding / spongiotrophoblast cell proliferation / positive regulation of skeletal muscle tissue growth / negative regulation of muscle cell differentiation / embryonic placenta morphogenesis / regulation of muscle cell differentiation / Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R) / IRS-related events triggered by IGF1R / insulin-like growth factor binding / genomic imprinting ...kringle domain binding / spongiotrophoblast cell proliferation / positive regulation of skeletal muscle tissue growth / negative regulation of muscle cell differentiation / embryonic placenta morphogenesis / regulation of muscle cell differentiation / Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R) / IRS-related events triggered by IGF1R / insulin-like growth factor binding / genomic imprinting / positive regulation of organ growth / exocrine pancreas development / positive regulation of multicellular organism growth / lysosomal transport / positive regulation of vascular endothelial cell proliferation / transmembrane receptor protein tyrosine kinase activator activity / positive regulation of activated T cell proliferation / D-mannose binding / positive regulation of cell division / endocytic vesicle / positive regulation of glycogen biosynthetic process / embryonic placenta development / SHC-related events triggered by IGF1R / positive regulation of insulin receptor signaling pathway / striated muscle cell differentiation / protein serine/threonine kinase activator activity / positive regulation of mitotic nuclear division / insulin-like growth factor receptor signaling pathway / platelet alpha granule lumen / phosphoprotein binding / animal organ morphogenesis / insulin-like growth factor receptor binding / growth factor activity / insulin receptor binding / trans-Golgi network / hormone activity / osteoblast differentiation / glucose metabolic process / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / positive regulation of peptidyl-tyrosine phosphorylation / integrin binding / late endosome / Platelet degranulation / insulin receptor signaling pathway / signaling receptor activity / in utero embryonic development / positive regulation of MAPK cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / receptor ligand activity / endosome membrane / Golgi membrane / positive regulation of cell population proliferation / regulation of DNA-templated transcription / Golgi apparatus / cell surface / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region / plasma membrane 類似検索 - 分子機能 | |||||||||
生物種 | ![]() ![]() ![]() ![]() ![]() | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 4.32 Å | |||||||||
![]() | Wang R / Qi X / Li X | |||||||||
![]() | ![]() タイトル: Marked structural rearrangement of mannose 6-phosphate/IGF2 receptor at different pH environments. 著者: Rong Wang / Xiaofeng Qi / Philip Schmiege / Elias Coutavas / Xiaochun Li / ![]() 要旨: Many cell surface receptors internalize their ligands and deliver them to endosomes, where the acidic pH causes the ligand to dissociate. The liberated receptor returns to the cell surface in a ...Many cell surface receptors internalize their ligands and deliver them to endosomes, where the acidic pH causes the ligand to dissociate. The liberated receptor returns to the cell surface in a process called receptor cycling. The structural basis for pH-dependent ligand dissociation is not well understood. In some receptors, the ligand binding domain is composed of multiple repeated sequences. The insulin-like growth factor 2 receptor (IGF2R) contains 15 β strand-rich repeat domains. The overall structure and the mechanism by which IGF2R binds IGF2 and releases it are unknown. We used cryo-EM to determine the structures of the IGF2R at pH 7.4 with IGF2 bound and at pH 4.5 in the ligand-dissociated state. The results reveal different arrangements of the receptor in different pH environments mediated by changes in the interactions between the repeated sequences. These results have implications for our understanding of ligand release from receptors in endocytic compartments. | |||||||||
履歴 |
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構造の表示
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構造ビューア | EMマップ: ![]() ![]() ![]() |
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-検証レポート
文書・要旨 | ![]() | 438.5 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 438 KB | 表示 | |
XML形式データ | ![]() | 6.5 KB | 表示 | |
CIF形式データ | ![]() | 7.4 KB | 表示 | |
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「今月の分子」の関連する項目 |
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マップ
ファイル | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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ボクセルのサイズ | X=Y=Z: 0.86 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
CCP4マップ ヘッダ情報:
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試料の構成要素
-全体 : IGFIIR and IGFII complex
全体 | 名称: IGFIIR and IGFII complex |
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要素 |
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-超分子 #1: IGFIIR and IGFII complex
超分子 | 名称: IGFIIR and IGFII complex / タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: #1-#2 |
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-超分子 #2: Cation-independent mannose-6-phosphate receptor
超分子 | 名称: Cation-independent mannose-6-phosphate receptor / タイプ: complex / ID: 2 / 親要素: 1 / 含まれる分子: #1 |
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由来(天然) | 生物種: ![]() ![]() |
-超分子 #3: Insulin-like growth factor II
超分子 | 名称: Insulin-like growth factor II / タイプ: complex / ID: 3 / 親要素: 1 / 含まれる分子: #2 |
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由来(天然) | 生物種: ![]() |
組換発現 | 生物種: ![]() ![]() |
-分子 #1: Cation-independent mannose-6-phosphate receptor
分子 | 名称: Cation-independent mannose-6-phosphate receptor / タイプ: protein_or_peptide / ID: 1 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: ![]() ![]() |
分子量 | 理論値: 274.830125 KDa |
配列 | 文字列: MEAAAGRSSH LGPAPAGRPP RCPLLLQLQL LLLLLLLPPG WVPGAAGTQG AEFPELCSYT WEAVDTKNNM LYKINICGNM GVAQCGPSS AVCMHDLKTD SFHSVGDSLL KTASRSLLEF NTTVNCKQQN HKIQSSITFL CGKTLGTPEF VTATDCVHYF E WRTTAACK ...文字列: MEAAAGRSSH LGPAPAGRPP RCPLLLQLQL LLLLLLLPPG WVPGAAGTQG AEFPELCSYT WEAVDTKNNM LYKINICGNM GVAQCGPSS AVCMHDLKTD SFHSVGDSLL KTASRSLLEF NTTVNCKQQN HKIQSSITFL CGKTLGTPEF VTATDCVHYF E WRTTAACK KNIFKANKEV PCYAFDRELK KHDLNPLIKT SGAYLVDDSD PDTSLFINVC RDIEVLRASS PQVRVCPTGA AA CLVRGDR AFDVGRPQEG LKLVSNDRLV LSYVKEGAGQ PDFCDGHSPA VTITFVCPSE RREGTIPKLT AKSNCRFEIE WVT EYACHR DYLESRSCSL SSAQHDVAVD LQPLSRVEAS DSLFYTSEAD EYTYYLSICG GSQAPICNKK DAAVCQVKKA DSTQ VKVAG RPQNLTLRYS DGDLTLIYFG GEECSSGFQR MSVINFECNQ TAGNNGRGAP VFTGEVDCTY FFTWDTKYAC VHEKE ALLC GVSDGKQRFD LSALARHSEL EQNWEAVDGS QREAEKKHFF INICHRVLQT GQARGCPEDA AVCAVDKNGS KNLGRF ISS PTREKGNIQL SYSDGDECGG GQKIITNITL MCKPGDLESA PVLTTSRADG CFYEFEWRTA AACVLSRTEG DNCTVFD SQ AGFSFDLTPL TKKDAYKVET DKYEFHINVC GPVSVGACPP DSGACQVSRS DRKSWNLGRS NAKLSYYDGM IQLTYRDG T PYNNEKRTPR ATLITFLCDR DAGVGFPEYQ EEDNSTYNFR WYTSYACPEE PLECIVTDPV TLDQYDLSRL AKSEGGPGG NWYSLDNGGA RSTWRKYYIN VCRPLNPVPG CDRYASACQM KYQGEQGSYS ETVSISNLGV AKTGPMVEDS GSLLLEYVNG SACTTSDQR RTTYTTRIHL VCSTGSLYTH PIFSLNWECV VSFLWNTAAA CPIRITTDID QVCSIKDPNS GYVFDLNPLN N SRGYVVLG IGKTFLFNVC GDMPACGTLD GKPASGCEAE VQMDDMKTLK PGRLVGLEKS LQLSTEGFIT LNYTGLPSHP NG RADAFII RFVCNDDVYP GTPKFLHQDI DSSLGIRDTF FEFETALACV PSPVDCQVTD PAGNEYDLSG LSKARKPWTA VDT FDEGKK RTFYLSVCTP LPYIPGCHGT AVGCCLVTED SKLNLGVVQI SPQVGANGSL SLVYVNGDKC KNQRFSTRIN LECA HTTGS PTFQLQNDCE YVFLWRTVEA CPVVRAEGDY CEVRDPRHGN LYNLIPLGLN DTVVRAGEYT YYFRVCGELT SGVCP TSDK SKVISSCQEK RGPQGFQKVA GLFNQKLTYE NGVLKMNYTG GDTCHKVYQR STTIFFYCDR STQAPVFLQE TSDCSY LFE WRTQYACPPY DLTECSFKNE AGETYDLSSL SRYSDNWEAV TGTGSTEHYL INVCKSLSPQ AGSDPCPPEA AVCLLGG PK PVNLGRVRDS PQWSQGLTLL KYVDGDLCPD QIRKKSTTIR FTCSESHVNS RPMFISAVED CEYTFSWPTA AACAVKSN V HDDCQVTNPA TGHLFDLSSL SGRAGFTAAY SEKGLVYLSV CGDNENCANG VGACFGQTRI SVGKASKRLT YVDQVLQLV YEGGSPCPSK TGLSYKSVIS FVCRPEVGPT NRPMLISLDK RTCTLFFSWH TPLACEQTTE CSVRNGSSLI DLSPLIHRTG GYEAYDESE DDGSDTSPDF YINICQPLNP MHGLACPAGT AVCKVPVDGP PIDIGRVAGP PILNPIANEV YLNFESSTPC L ADRHFNYT SLITFHCKRG VSMGTPKLLR TSVCDFVFEW ETPLVCPDEV KTDGCSLTDE QLYYSFNLSS LSKSTFKVTR GP HTYSVGV CTAAAGLDEG GCKDGAVCLL SGSKGASFGR LASMKLDYRH QDEAVILSYA NGDTCPPETE DGEPCVFPFV FNG KSYEEC VVESRARLWC ATTANYDRDH EWGFCKHSTS HRTSVIIFKC DEDADVGRPQ VFSEVRGCEV TFEWKTKVVC PPKK MECKF VQKHRTYDLR LLSSLTGSWS FVHNGASYYI NLCQKIYKGP QDCSERASVC KKSTSGEVQV LGLVHTQKLD VVDDR VIVT YSKGHYCGDN KTASAVIELT CAKTVGRPSF TRFDVDSCTY HFSWDSRAAC AVKPQEVQMV NGTITNPANG RSFSLG DIY FKRFSASGDV RTNGDRYIYE IQLSSITGSS SPACSGASIC QRKANDQHFS RKVGTSNQTR YYVQDGDLDV VFTSSSK CG KDKTKSVSST IFFHCDPLVK DGIPEFSHET ADCQYLFSWH TSAVCPLGAG FDEEIAGDDA QEHKGLSERS QAVGAVLS L LLVALTACLL TLLLYKKERR EMVMSRLTNC CRRSANVSYK YSKVNKEEEA DENETEWLME EIQPPAPRPG KEGQENGHV AAKSVRAADT LSALHGDEQD SEDEVLTLPE VKVRPPGRAP GAEGGPPLRP LPRKAPPPLR ADDRVGLVRG EPARRGRPRA AATPISTFH DDSDEDLLHV |
-分子 #2: Insulin-like growth factor II
分子 | 名称: Insulin-like growth factor II / タイプ: protein_or_peptide / ID: 2 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: ![]() |
分子量 | 理論値: 7.615667 KDa |
組換発現 | 生物種: ![]() ![]() |
配列 | 文字列: MAYRPSETLC GGELVDTLQF VCGDRGFYFS RPASRVSRRS RGIVEECCFR SCDLALLETY CATPAKSE |
-分子 #3: 2-acetamido-2-deoxy-beta-D-glucopyranose
分子 | 名称: 2-acetamido-2-deoxy-beta-D-glucopyranose / タイプ: ligand / ID: 3 / コピー数: 7 / 式: NAG |
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分子量 | 理論値: 221.208 Da |
Chemical component information | ![]() ChemComp-NAG: |
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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![]() | 単粒子再構成法 |
試料の集合状態 | particle |
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試料調製
緩衝液 | pH: 7.4 |
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凍結 | 凍結剤: ETHANE |
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電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
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撮影 | フィルム・検出器のモデル: GATAN K3 (6k x 4k) / 平均電子線量: 100.0 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: ![]() |
電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: DARK FIELD |
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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画像解析
最終 再構成 | 解像度のタイプ: BY AUTHOR / 解像度: 4.32 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 75821 |
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初期 角度割当 | タイプ: ANGULAR RECONSTITUTION |
最終 角度割当 | タイプ: ANGULAR RECONSTITUTION |