Crystal Structure of the Catalytic Domain of Human ADAM33
Adam33 is a putative asthma susceptibility gene encoding for a membrane-anchored metalloprotease belonging to the ADAM family. The ADAMs (a disintegrin and metalloprotease) are a family of glycoproteins implicated in cell-cell interactions, cell fusion, and cell signaling. We have determined the cry...
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Veröffentlicht in: | Journal of molecular biology 2004-01, Vol.335 (1), p.129-137 |
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creator | Orth, Peter Reichert, Paul Wang, Wenyan Prosise, Winifred W. Yarosh-Tomaine, Taisa Hammond, Gerald Ingram, Richard N. Xiao, Li Mirza, Urooj A. Zou, Jun Strickland, Corey Taremi, S.Shane Le, Hung V. Madison, Vincent |
description | Adam33 is a putative asthma susceptibility gene encoding for a membrane-anchored metalloprotease belonging to the ADAM family. The ADAMs (a disintegrin and metalloprotease) are a family of glycoproteins implicated in cell-cell interactions, cell fusion, and cell signaling. We have determined the crystal structure of the Adam33 catalytic domain in complex with the inhibitor marimastat and the inhibitor-free form. The structures reveal the polypeptide fold and active site environment resembling that of other metalloproteases. The substrate-binding site contains unique features that allow the structure-based design of specific inhibitors of this enzyme. |
doi_str_mv | 10.1016/j.jmb.2003.10.037 |
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The ADAMs (a disintegrin and metalloprotease) are a family of glycoproteins implicated in cell-cell interactions, cell fusion, and cell signaling. We have determined the crystal structure of the Adam33 catalytic domain in complex with the inhibitor marimastat and the inhibitor-free form. The structures reveal the polypeptide fold and active site environment resembling that of other metalloproteases. The substrate-binding site contains unique features that allow the structure-based design of specific inhibitors of this enzyme.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/j.jmb.2003.10.037</identifier><identifier>PMID: 14659745</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>ADAM Proteins ; ADAM33 ; ADAM33 protein ; Amino Acid Sequence ; asthma ; Catalytic Domain ; Crystallography, X-Ray ; Enzyme Inhibitors - chemistry ; Humans ; Hydroxamic Acids - chemistry ; marimastat ; Metalloendopeptidases - chemistry ; Metalloendopeptidases - genetics ; metalloprotease ; Models, Molecular ; Molecular Structure ; Mutation ; Protein Binding ; Protein Structure, Tertiary ; Sequence Alignment ; X-ray structure</subject><ispartof>Journal of molecular biology, 2004-01, Vol.335 (1), p.129-137</ispartof><rights>2003 Elsevier Science Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c448t-8e7eb83c52aac8b89d7541fd36015a00a936519760a331f558bf0f709fbd6c393</citedby><cites>FETCH-LOGICAL-c448t-8e7eb83c52aac8b89d7541fd36015a00a936519760a331f558bf0f709fbd6c393</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0022283603013135$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14659745$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Orth, Peter</creatorcontrib><creatorcontrib>Reichert, Paul</creatorcontrib><creatorcontrib>Wang, Wenyan</creatorcontrib><creatorcontrib>Prosise, Winifred W.</creatorcontrib><creatorcontrib>Yarosh-Tomaine, Taisa</creatorcontrib><creatorcontrib>Hammond, Gerald</creatorcontrib><creatorcontrib>Ingram, Richard N.</creatorcontrib><creatorcontrib>Xiao, Li</creatorcontrib><creatorcontrib>Mirza, Urooj A.</creatorcontrib><creatorcontrib>Zou, Jun</creatorcontrib><creatorcontrib>Strickland, Corey</creatorcontrib><creatorcontrib>Taremi, S.Shane</creatorcontrib><creatorcontrib>Le, Hung V.</creatorcontrib><creatorcontrib>Madison, Vincent</creatorcontrib><title>Crystal Structure of the Catalytic Domain of Human ADAM33</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>Adam33 is a putative asthma susceptibility gene encoding for a membrane-anchored metalloprotease belonging to the ADAM family. The ADAMs (a disintegrin and metalloprotease) are a family of glycoproteins implicated in cell-cell interactions, cell fusion, and cell signaling. We have determined the crystal structure of the Adam33 catalytic domain in complex with the inhibitor marimastat and the inhibitor-free form. The structures reveal the polypeptide fold and active site environment resembling that of other metalloproteases. The substrate-binding site contains unique features that allow the structure-based design of specific inhibitors of this enzyme.</description><subject>ADAM Proteins</subject><subject>ADAM33</subject><subject>ADAM33 protein</subject><subject>Amino Acid Sequence</subject><subject>asthma</subject><subject>Catalytic Domain</subject><subject>Crystallography, X-Ray</subject><subject>Enzyme Inhibitors - chemistry</subject><subject>Humans</subject><subject>Hydroxamic Acids - chemistry</subject><subject>marimastat</subject><subject>Metalloendopeptidases - chemistry</subject><subject>Metalloendopeptidases - genetics</subject><subject>metalloprotease</subject><subject>Models, Molecular</subject><subject>Molecular Structure</subject><subject>Mutation</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Sequence Alignment</subject><subject>X-ray structure</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkD1PwzAURS0EoqXwA1hQJraE5zh2bDFVLVCkIgZgthzHEYnyUWwHqf8eR63EBtPTuzr3DgehawwJBszumqTpiiQFIOFPgOQnaI6Bi5gzwk_RHCBN45QTNkMXzjUAQEnGz9EMZ4yKPKNzJFZ277xqozdvR-1Ha6KhivyniVYqxHtf62g9dKrup3wzdqqPluvlCyGX6KxSrTNXx7tAH48P76tNvH19el4tt7HOMu5jbnJTcKJpqpTmBRdlTjNclYQBpgpACcIoFjkDRQiuKOVFBVUOoipKpokgC3R72N3Z4Ws0zsuudtq0rerNMDqZY8qyXPB_QSzSQAoWQHwAtR2cs6aSO1t3yu4lBjmJlY0MYuUkdoqC2NC5OY6PRWfK38bRZADuD4AJLr5rY6XTtem1KWtrtJflUP8x_wM1iIX9</recordid><startdate>20040102</startdate><enddate>20040102</enddate><creator>Orth, Peter</creator><creator>Reichert, Paul</creator><creator>Wang, Wenyan</creator><creator>Prosise, Winifred W.</creator><creator>Yarosh-Tomaine, Taisa</creator><creator>Hammond, Gerald</creator><creator>Ingram, Richard N.</creator><creator>Xiao, Li</creator><creator>Mirza, Urooj A.</creator><creator>Zou, Jun</creator><creator>Strickland, Corey</creator><creator>Taremi, S.Shane</creator><creator>Le, Hung V.</creator><creator>Madison, Vincent</creator><general>Elsevier Ltd</general><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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20040102</creationdate><title>Crystal Structure of the Catalytic Domain of Human ADAM33</title><author>Orth, Peter ; Reichert, Paul ; Wang, Wenyan ; Prosise, Winifred W. ; Yarosh-Tomaine, Taisa ; Hammond, Gerald ; Ingram, Richard N. ; Xiao, Li ; Mirza, Urooj A. ; Zou, Jun ; Strickland, Corey ; Taremi, S.Shane ; Le, Hung V. ; Madison, Vincent</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c448t-8e7eb83c52aac8b89d7541fd36015a00a936519760a331f558bf0f709fbd6c393</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>ADAM Proteins</topic><topic>ADAM33</topic><topic>ADAM33 protein</topic><topic>Amino Acid Sequence</topic><topic>asthma</topic><topic>Catalytic Domain</topic><topic>Crystallography, X-Ray</topic><topic>Enzyme Inhibitors - chemistry</topic><topic>Humans</topic><topic>Hydroxamic Acids - chemistry</topic><topic>marimastat</topic><topic>Metalloendopeptidases - chemistry</topic><topic>Metalloendopeptidases - genetics</topic><topic>metalloprotease</topic><topic>Models, Molecular</topic><topic>Molecular Structure</topic><topic>Mutation</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Sequence Alignment</topic><topic>X-ray structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Orth, Peter</creatorcontrib><creatorcontrib>Reichert, Paul</creatorcontrib><creatorcontrib>Wang, Wenyan</creatorcontrib><creatorcontrib>Prosise, Winifred W.</creatorcontrib><creatorcontrib>Yarosh-Tomaine, Taisa</creatorcontrib><creatorcontrib>Hammond, Gerald</creatorcontrib><creatorcontrib>Ingram, Richard N.</creatorcontrib><creatorcontrib>Xiao, Li</creatorcontrib><creatorcontrib>Mirza, Urooj A.</creatorcontrib><creatorcontrib>Zou, Jun</creatorcontrib><creatorcontrib>Strickland, Corey</creatorcontrib><creatorcontrib>Taremi, S.Shane</creatorcontrib><creatorcontrib>Le, Hung V.</creatorcontrib><creatorcontrib>Madison, Vincent</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Orth, Peter</au><au>Reichert, Paul</au><au>Wang, Wenyan</au><au>Prosise, Winifred W.</au><au>Yarosh-Tomaine, Taisa</au><au>Hammond, Gerald</au><au>Ingram, Richard N.</au><au>Xiao, Li</au><au>Mirza, Urooj A.</au><au>Zou, Jun</au><au>Strickland, Corey</au><au>Taremi, S.Shane</au><au>Le, Hung V.</au><au>Madison, Vincent</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal Structure of the Catalytic Domain of Human ADAM33</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>2004-01-02</date><risdate>2004</risdate><volume>335</volume><issue>1</issue><spage>129</spage><epage>137</epage><pages>129-137</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><abstract>Adam33 is a putative asthma susceptibility gene encoding for a membrane-anchored metalloprotease belonging to the ADAM family. The ADAMs (a disintegrin and metalloprotease) are a family of glycoproteins implicated in cell-cell interactions, cell fusion, and cell signaling. We have determined the crystal structure of the Adam33 catalytic domain in complex with the inhibitor marimastat and the inhibitor-free form. The structures reveal the polypeptide fold and active site environment resembling that of other metalloproteases. The substrate-binding site contains unique features that allow the structure-based design of specific inhibitors of this enzyme.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>14659745</pmid><doi>10.1016/j.jmb.2003.10.037</doi><tpages>9</tpages></addata></record> |
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subjects | ADAM Proteins ADAM33 ADAM33 protein Amino Acid Sequence asthma Catalytic Domain Crystallography, X-Ray Enzyme Inhibitors - chemistry Humans Hydroxamic Acids - chemistry marimastat Metalloendopeptidases - chemistry Metalloendopeptidases - genetics metalloprotease Models, Molecular Molecular Structure Mutation Protein Binding Protein Structure, Tertiary Sequence Alignment X-ray structure |
title | Crystal Structure of the Catalytic Domain of Human ADAM33 |
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