Three-dimensional Structure of Transporter Associated with Antigen Processing (TAP) Obtained by Single Particle Image Analysis
The transporter associated with antigen processing (TAP) is an ATP binding cassette transporter responsible for peptide translocation into the lumen of the endoplasmic reticulum for assembly with major histocompatibility complex class I molecules. Immunoaffinity-purified TAP particles comprising TAP...
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| Veröffentlicht in: | The Journal of biological chemistry 2001-12, Vol.276 (49), p.46054-46063 |
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| container_end_page | 46063 |
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| container_issue | 49 |
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| container_title | The Journal of biological chemistry |
| container_volume | 276 |
| creator | Velarde, Giles Ford, Robert C. Rosenberg, Mark F. Powis, Simon J. |
| description | The transporter associated with antigen processing (TAP) is an ATP binding cassette transporter responsible for peptide translocation into the lumen of the endoplasmic reticulum for assembly with major histocompatibility complex class I molecules. Immunoaffinity-purified TAP particles comprising TAP1 and TAP2 polypeptides, and TAP2 particles alone were characterized after detergent solubilization and studied by electron microscopy. Projection structures of TAP1+2 particles reveal a molecule ∼10 nm across with a deeply staining central region, whereas TAP2 molecules are smaller in projection. A three-dimensional structure of TAP reveals it is isolated as a single heterodimeric complex, with the TAP1 and TAP2 subunits combining to create a central 3-nm-diameter pocket on the predicted endoplasmic reticulum-lumenal side. Its structural similarity to other ABC transporters demonstrates a common tertiary structure for this diverse family of membrane proteins. |
| doi_str_mv | 10.1074/jbc.M108435200 |
| format | Article |
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Immunoaffinity-purified TAP particles comprising TAP1 and TAP2 polypeptides, and TAP2 particles alone were characterized after detergent solubilization and studied by electron microscopy. Projection structures of TAP1+2 particles reveal a molecule ∼10 nm across with a deeply staining central region, whereas TAP2 molecules are smaller in projection. A three-dimensional structure of TAP reveals it is isolated as a single heterodimeric complex, with the TAP1 and TAP2 subunits combining to create a central 3-nm-diameter pocket on the predicted endoplasmic reticulum-lumenal side. 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Immunoaffinity-purified TAP particles comprising TAP1 and TAP2 polypeptides, and TAP2 particles alone were characterized after detergent solubilization and studied by electron microscopy. Projection structures of TAP1+2 particles reveal a molecule ∼10 nm across with a deeply staining central region, whereas TAP2 molecules are smaller in projection. A three-dimensional structure of TAP reveals it is isolated as a single heterodimeric complex, with the TAP1 and TAP2 subunits combining to create a central 3-nm-diameter pocket on the predicted endoplasmic reticulum-lumenal side. Its structural similarity to other ABC transporters demonstrates a common tertiary structure for this diverse family of membrane proteins.</description><subject>ABC transporter</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antigens - metabolism</subject><subject>ATP-Binding Cassette Transporters - chemistry</subject><subject>ATP-Binding Cassette Transporters - isolation & purification</subject><subject>ATP-Binding Cassette Transporters - metabolism</subject><subject>Cell Line</subject><subject>Flow Cytometry</subject><subject>Protein Conformation</subject><subject>Rats</subject><subject>TAP1 protein</subject><subject>TAP2 protein</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFr3DAQhUVpabZJrz0WHUpoDt5IsmxZxyW0SSAlC9lCb0KSx2sF29pKcsNe8tursAs5lc5lhpnvDcM8hD5RsqRE8MtHY5c_KGl4WTFC3qBFrsuirOivt2hBCKOFZFVzgj7E-EhycEnfoxNKK1kJXi_Q86YPAEXrRpii85Me8EMKs01zAOw7vAl6ijsfEgS8itFbpxO0-MmlHq-m5LYw4XXwFmJ00xZ_3azWF_jeJO2mjJk9fsjtAfBah-RsLm5HvYUs1cM-uniG3nV6iPDxmE_Rz-_fNlc3xd399e3V6q6wnJNUMN5Qw0GUtKNgoDS0IsCF5ASE1LpljEOe18JUREtua1oKEF1rmbVaAilP0flh7y743zPEpEYXLQyDnsDPUQlWUlnK-r8gbRiRhL-AywNog48xQKd2wY067BUl6sUala1Rr9Zkwefj5tmM0L7iRy8y8OUA9G7bP7kAyjhvexgVE7XiUvGaVDxjzQGD_K8_DoKK1sFkoc0Sm1Tr3b9O-As6aKm9</recordid><startdate>20011207</startdate><enddate>20011207</enddate><creator>Velarde, Giles</creator><creator>Ford, Robert C.</creator><creator>Rosenberg, Mark F.</creator><creator>Powis, Simon J.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</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>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20011207</creationdate><title>Three-dimensional Structure of Transporter Associated with Antigen Processing (TAP) Obtained by Single Particle Image Analysis</title><author>Velarde, Giles ; Ford, Robert C. ; Rosenberg, Mark F. ; Powis, Simon J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c440t-2481b4e731f1ebe3b150e47940e79aad224eb4e67b50a94c6137e7fdc2cca9e03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>ABC transporter</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antigens - metabolism</topic><topic>ATP-Binding Cassette Transporters - chemistry</topic><topic>ATP-Binding Cassette Transporters - isolation & purification</topic><topic>ATP-Binding Cassette Transporters - metabolism</topic><topic>Cell Line</topic><topic>Flow Cytometry</topic><topic>Protein Conformation</topic><topic>Rats</topic><topic>TAP1 protein</topic><topic>TAP2 protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Velarde, Giles</creatorcontrib><creatorcontrib>Ford, Robert C.</creatorcontrib><creatorcontrib>Rosenberg, Mark F.</creatorcontrib><creatorcontrib>Powis, Simon J.</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>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Velarde, Giles</au><au>Ford, Robert C.</au><au>Rosenberg, Mark F.</au><au>Powis, Simon J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Three-dimensional Structure of Transporter Associated with Antigen Processing (TAP) Obtained by Single Particle Image Analysis</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2001-12-07</date><risdate>2001</risdate><volume>276</volume><issue>49</issue><spage>46054</spage><epage>46063</epage><pages>46054-46063</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The transporter associated with antigen processing (TAP) is an ATP binding cassette transporter responsible for peptide translocation into the lumen of the endoplasmic reticulum for assembly with major histocompatibility complex class I molecules. 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| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | ABC transporter Amino Acid Sequence Animals Antigens - metabolism ATP-Binding Cassette Transporters - chemistry ATP-Binding Cassette Transporters - isolation & purification ATP-Binding Cassette Transporters - metabolism Cell Line Flow Cytometry Protein Conformation Rats TAP1 protein TAP2 protein |
| title | Three-dimensional Structure of Transporter Associated with Antigen Processing (TAP) Obtained by Single Particle Image Analysis |
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