Crystal Structure of Human Lectin-like, Oxidized Low-Density Lipoprotein Receptor 1 Ligand Binding Domain and Its Ligand Recognition Mode to OxLDL
Lectin-like, oxidized low-density lipoprotein (LDL) receptor 1, LOX-1, is the major receptor for oxidized LDL (OxLDL) in endothelial cells. We have determined the crystal structure of the ligand binding domain of LOX-1, with a short stalk region connecting the domain to the membrane-spanning region,...
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| Veröffentlicht in: | Structure (London) 2005-06, Vol.13 (6), p.905-917 |
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| creator | Ohki, Izuru Ishigaki, Tomoko Oyama, Takuji Matsunaga, Shigeru Xie, Qiuhong Ohnishi-Kameyama, Mayumi Murata, Takashi Tsuchiya, Daisuke Machida, Sachiko Morikawa, Kousuke Tate, Shin-ichi |
| description | Lectin-like, oxidized low-density lipoprotein (LDL) receptor 1, LOX-1, is the major receptor for oxidized LDL (OxLDL) in endothelial cells. We have determined the crystal structure of the ligand binding domain of LOX-1, with a short stalk region connecting the domain to the membrane-spanning region, as a homodimer linked by an interchain disulfide bond. In vivo assays with LOX-1 mutants revealed that the “basic spine,” consisting of linearly aligned arginine residues spanning over the dimer surface, is responsible for ligand binding. Single amino acid substitution in the dimer interface caused a severe reduction in LOX-1 binding activity, suggesting that the correct dimer arrangement is crucial for binding to OxLDL. Based on the LDL model structure, possible binding modes of LOX-1 to OxLDL are proposed. |
| doi_str_mv | 10.1016/j.str.2005.03.016 |
| format | Article |
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We have determined the crystal structure of the ligand binding domain of LOX-1, with a short stalk region connecting the domain to the membrane-spanning region, as a homodimer linked by an interchain disulfide bond. In vivo assays with LOX-1 mutants revealed that the “basic spine,” consisting of linearly aligned arginine residues spanning over the dimer surface, is responsible for ligand binding. Single amino acid substitution in the dimer interface caused a severe reduction in LOX-1 binding activity, suggesting that the correct dimer arrangement is crucial for binding to OxLDL. Based on the LDL model structure, possible binding modes of LOX-1 to OxLDL are proposed.</description><identifier>ISSN: 0969-2126</identifier><identifier>EISSN: 1878-4186</identifier><identifier>DOI: 10.1016/j.str.2005.03.016</identifier><identifier>PMID: 15939022</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Arginine - chemistry ; Binding Sites ; CHO Cells ; Conserved Sequence ; Cricetinae ; Cricetulus ; Crystallography, X-Ray ; Cysteine - chemistry ; Dimerization ; Disulfides - chemistry ; Humans ; Hydrogen Bonding ; Ligands ; Lipoproteins, LDL - chemistry ; Lipoproteins, LDL - metabolism ; Models, Chemical ; Models, Molecular ; Molecular Sequence Data ; Protein Binding ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Receptors, LDL - chemistry ; Receptors, LDL - genetics ; Receptors, LDL - metabolism ; Receptors, Oxidized LDL ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; Scavenger Receptors, Class E ; Sequence Homology, Amino Acid</subject><ispartof>Structure (London), 2005-06, Vol.13 (6), p.905-917</ispartof><rights>2005 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c460t-5b1b9f0d4075f449439065cbef2ec54e5b71dbac477332104b1eb054b72b862b3</citedby><cites>FETCH-LOGICAL-c460t-5b1b9f0d4075f449439065cbef2ec54e5b71dbac477332104b1eb054b72b862b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.str.2005.03.016$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15939022$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ohki, Izuru</creatorcontrib><creatorcontrib>Ishigaki, Tomoko</creatorcontrib><creatorcontrib>Oyama, Takuji</creatorcontrib><creatorcontrib>Matsunaga, Shigeru</creatorcontrib><creatorcontrib>Xie, Qiuhong</creatorcontrib><creatorcontrib>Ohnishi-Kameyama, Mayumi</creatorcontrib><creatorcontrib>Murata, Takashi</creatorcontrib><creatorcontrib>Tsuchiya, Daisuke</creatorcontrib><creatorcontrib>Machida, Sachiko</creatorcontrib><creatorcontrib>Morikawa, Kousuke</creatorcontrib><creatorcontrib>Tate, Shin-ichi</creatorcontrib><title>Crystal Structure of Human Lectin-like, Oxidized Low-Density Lipoprotein Receptor 1 Ligand Binding Domain and Its Ligand Recognition Mode to OxLDL</title><title>Structure (London)</title><addtitle>Structure</addtitle><description>Lectin-like, oxidized low-density lipoprotein (LDL) receptor 1, LOX-1, is the major receptor for oxidized LDL (OxLDL) in endothelial cells. We have determined the crystal structure of the ligand binding domain of LOX-1, with a short stalk region connecting the domain to the membrane-spanning region, as a homodimer linked by an interchain disulfide bond. In vivo assays with LOX-1 mutants revealed that the “basic spine,” consisting of linearly aligned arginine residues spanning over the dimer surface, is responsible for ligand binding. Single amino acid substitution in the dimer interface caused a severe reduction in LOX-1 binding activity, suggesting that the correct dimer arrangement is crucial for binding to OxLDL. Based on the LDL model structure, possible binding modes of LOX-1 to OxLDL are proposed.</description><subject>Amino Acid Sequence</subject><subject>Amino Acid Substitution</subject><subject>Animals</subject><subject>Arginine - chemistry</subject><subject>Binding Sites</subject><subject>CHO Cells</subject><subject>Conserved Sequence</subject><subject>Cricetinae</subject><subject>Cricetulus</subject><subject>Crystallography, X-Ray</subject><subject>Cysteine - chemistry</subject><subject>Dimerization</subject><subject>Disulfides - chemistry</subject><subject>Humans</subject><subject>Hydrogen Bonding</subject><subject>Ligands</subject><subject>Lipoproteins, LDL - chemistry</subject><subject>Lipoproteins, LDL - metabolism</subject><subject>Models, Chemical</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Protein Binding</subject><subject>Protein Folding</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Receptors, LDL - chemistry</subject><subject>Receptors, LDL - genetics</subject><subject>Receptors, LDL - metabolism</subject><subject>Receptors, Oxidized LDL</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>Scavenger Receptors, Class E</subject><subject>Sequence Homology, Amino Acid</subject><issn>0969-2126</issn><issn>1878-4186</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc2OEzEQhC0EYsPCA3BBPnFihrbH8ydOkAC70qCV-DlbY7sncpjYwfYA4TF4YhwliBsnS-Wvq1VdhDxlUDJgzctdGVMoOUBdQlVm5R5Zsa7tCsG65j5ZQd_0BWe8uSKPYtwBAK8BHpIrVvdVD5yvyO91OMY0zvRTCotOS0DqJ3qz7EdHB9TJumK2X_EFvftpjf2Fhg7-R7FBF2060sEe_CH4hNbRj6jxkHygLMvb0Rn6xjpj3ZZu_H7MwEm6TfHvb-b91tlkvaMfvEGafF4ybIbH5ME0zhGfXN5r8uXd28_rm2K4e3-7fj0UWjSQilox1U9gBLT1JEQvcqKm1gonjroWWKuWGTVq0bZVxRkIxVBBLVTLVddwVV2T52ffnODbgjHJvY0a53l06Jcom7aHruuaDLIzqIOPMeAkD8Hux3CUDOSpCLmTuQh5KkJCJbOSZ55dzBe1R_Nv4nL5DLw6A5gjfrcYZNQWnUZjQ767NN7-x_4PFHqZvg</recordid><startdate>20050601</startdate><enddate>20050601</enddate><creator>Ohki, Izuru</creator><creator>Ishigaki, Tomoko</creator><creator>Oyama, Takuji</creator><creator>Matsunaga, Shigeru</creator><creator>Xie, Qiuhong</creator><creator>Ohnishi-Kameyama, Mayumi</creator><creator>Murata, Takashi</creator><creator>Tsuchiya, Daisuke</creator><creator>Machida, Sachiko</creator><creator>Morikawa, Kousuke</creator><creator>Tate, Shin-ichi</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20050601</creationdate><title>Crystal Structure of Human Lectin-like, Oxidized Low-Density Lipoprotein Receptor 1 Ligand Binding Domain and Its Ligand Recognition Mode to OxLDL</title><author>Ohki, Izuru ; Ishigaki, Tomoko ; Oyama, Takuji ; Matsunaga, Shigeru ; Xie, Qiuhong ; Ohnishi-Kameyama, Mayumi ; Murata, Takashi ; Tsuchiya, Daisuke ; Machida, Sachiko ; Morikawa, Kousuke ; Tate, Shin-ichi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c460t-5b1b9f0d4075f449439065cbef2ec54e5b71dbac477332104b1eb054b72b862b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acid Substitution</topic><topic>Animals</topic><topic>Arginine - chemistry</topic><topic>Binding Sites</topic><topic>CHO Cells</topic><topic>Conserved Sequence</topic><topic>Cricetinae</topic><topic>Cricetulus</topic><topic>Crystallography, X-Ray</topic><topic>Cysteine - chemistry</topic><topic>Dimerization</topic><topic>Disulfides - chemistry</topic><topic>Humans</topic><topic>Hydrogen Bonding</topic><topic>Ligands</topic><topic>Lipoproteins, LDL - chemistry</topic><topic>Lipoproteins, LDL - metabolism</topic><topic>Models, Chemical</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Protein Binding</topic><topic>Protein Folding</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>Receptors, LDL - chemistry</topic><topic>Receptors, LDL - genetics</topic><topic>Receptors, LDL - metabolism</topic><topic>Receptors, Oxidized LDL</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - metabolism</topic><topic>Scavenger Receptors, Class E</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ohki, Izuru</creatorcontrib><creatorcontrib>Ishigaki, Tomoko</creatorcontrib><creatorcontrib>Oyama, Takuji</creatorcontrib><creatorcontrib>Matsunaga, Shigeru</creatorcontrib><creatorcontrib>Xie, Qiuhong</creatorcontrib><creatorcontrib>Ohnishi-Kameyama, Mayumi</creatorcontrib><creatorcontrib>Murata, Takashi</creatorcontrib><creatorcontrib>Tsuchiya, Daisuke</creatorcontrib><creatorcontrib>Machida, Sachiko</creatorcontrib><creatorcontrib>Morikawa, Kousuke</creatorcontrib><creatorcontrib>Tate, Shin-ichi</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Structure (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ohki, Izuru</au><au>Ishigaki, Tomoko</au><au>Oyama, Takuji</au><au>Matsunaga, Shigeru</au><au>Xie, Qiuhong</au><au>Ohnishi-Kameyama, Mayumi</au><au>Murata, Takashi</au><au>Tsuchiya, Daisuke</au><au>Machida, Sachiko</au><au>Morikawa, Kousuke</au><au>Tate, Shin-ichi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal Structure of Human Lectin-like, Oxidized Low-Density Lipoprotein Receptor 1 Ligand Binding Domain and Its Ligand Recognition Mode to OxLDL</atitle><jtitle>Structure (London)</jtitle><addtitle>Structure</addtitle><date>2005-06-01</date><risdate>2005</risdate><volume>13</volume><issue>6</issue><spage>905</spage><epage>917</epage><pages>905-917</pages><issn>0969-2126</issn><eissn>1878-4186</eissn><abstract>Lectin-like, oxidized low-density lipoprotein (LDL) receptor 1, LOX-1, is the major receptor for oxidized LDL (OxLDL) in endothelial cells. We have determined the crystal structure of the ligand binding domain of LOX-1, with a short stalk region connecting the domain to the membrane-spanning region, as a homodimer linked by an interchain disulfide bond. In vivo assays with LOX-1 mutants revealed that the “basic spine,” consisting of linearly aligned arginine residues spanning over the dimer surface, is responsible for ligand binding. Single amino acid substitution in the dimer interface caused a severe reduction in LOX-1 binding activity, suggesting that the correct dimer arrangement is crucial for binding to OxLDL. Based on the LDL model structure, possible binding modes of LOX-1 to OxLDL are proposed.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15939022</pmid><doi>10.1016/j.str.2005.03.016</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Structure (London), 2005-06, Vol.13 (6), p.905-917 |
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| source | MEDLINE; Cell Press Free Archives; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Amino Acid Substitution Animals Arginine - chemistry Binding Sites CHO Cells Conserved Sequence Cricetinae Cricetulus Crystallography, X-Ray Cysteine - chemistry Dimerization Disulfides - chemistry Humans Hydrogen Bonding Ligands Lipoproteins, LDL - chemistry Lipoproteins, LDL - metabolism Models, Chemical Models, Molecular Molecular Sequence Data Protein Binding Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Receptors, LDL - chemistry Receptors, LDL - genetics Receptors, LDL - metabolism Receptors, Oxidized LDL Recombinant Proteins - chemistry Recombinant Proteins - metabolism Scavenger Receptors, Class E Sequence Homology, Amino Acid |
| title | Crystal Structure of Human Lectin-like, Oxidized Low-Density Lipoprotein Receptor 1 Ligand Binding Domain and Its Ligand Recognition Mode to OxLDL |
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