Structural and Phylogenetic Relationships among Plant and Animal Cystatins
The plant cystatins or phytocystatins (PhyCys) are cysteine proteinase inhibitors containing the QxVxG motif and have been placed in the cystatin superfamily of proteins. The primary sequences of PhyCys have a high degree of homology with the members of the cystatin family, but they resemble stefins...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1998-11, Vol.359 (1), p.24-30 |
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| container_title | Archives of biochemistry and biophysics |
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| creator | Margis, Rogério Reis, Emerson M. Villeret, Vincent |
| description | The plant cystatins or phytocystatins (PhyCys) are cysteine proteinase inhibitors containing the QxVxG motif and have been placed in the cystatin superfamily of proteins. The primary sequences of PhyCys have a high degree of homology with the members of the cystatin family, but they resemble stefins by the absence of disulfide bonds and cysteine residues. A multialignment and a phylogenetic analysis of 63 cystatins, 32 of which are PhyCys, demonstrate that all PhyCys cluster in a major evolutionary tree branch and support the classification of PhyCys as a new cystatin family. The PhyCys also possess a specific consensus sequence [LVI]-[AGT]-[RKE]-[FY]-[AS]-[VI]-x-[EDQV]-[HYFQ]-N placed on the region corresponding to a predictable amino-terminal α-helix. This sequence can be used to specifically identify PhyCys on protein data banks and to differentiate them from the other members of the superfamily. |
| doi_str_mv | 10.1006/abbi.1998.0875 |
| format | Article |
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The primary sequences of PhyCys have a high degree of homology with the members of the cystatin family, but they resemble stefins by the absence of disulfide bonds and cysteine residues. A multialignment and a phylogenetic analysis of 63 cystatins, 32 of which are PhyCys, demonstrate that all PhyCys cluster in a major evolutionary tree branch and support the classification of PhyCys as a new cystatin family. The PhyCys also possess a specific consensus sequence [LVI]-[AGT]-[RKE]-[FY]-[AS]-[VI]-x-[EDQV]-[HYFQ]-N placed on the region corresponding to a predictable amino-terminal α-helix. This sequence can be used to specifically identify PhyCys on protein data banks and to differentiate them from the other members of the superfamily.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1006/abbi.1998.0875</identifier><identifier>PMID: 9799556</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Conserved Sequence ; cystatins ; Cystatins - chemistry ; Cystatins - genetics ; Cysteine - chemistry ; cysteine proteinase inhibitors ; Humans ; Models, Molecular ; Molecular Sequence Data ; Phenylalanine - chemistry ; Phylogeny ; phytocystatins ; Plants - chemistry ; Plants - genetics ; Sequence Homology, Amino Acid ; stefins</subject><ispartof>Archives of biochemistry and biophysics, 1998-11, Vol.359 (1), p.24-30</ispartof><rights>1998 Academic Press</rights><rights>Copyright 1998 Academic Press.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c405t-53f6b26e75ce9148562e095520c9bde2b04bb935a8200d8889f0e3e16810cf973</citedby><cites>FETCH-LOGICAL-c405t-53f6b26e75ce9148562e095520c9bde2b04bb935a8200d8889f0e3e16810cf973</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/abbi.1998.0875$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3549,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9799556$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Margis, Rogério</creatorcontrib><creatorcontrib>Reis, Emerson M.</creatorcontrib><creatorcontrib>Villeret, Vincent</creatorcontrib><title>Structural and Phylogenetic Relationships among Plant and Animal Cystatins</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The plant cystatins or phytocystatins (PhyCys) are cysteine proteinase inhibitors containing the QxVxG motif and have been placed in the cystatin superfamily of proteins. The primary sequences of PhyCys have a high degree of homology with the members of the cystatin family, but they resemble stefins by the absence of disulfide bonds and cysteine residues. A multialignment and a phylogenetic analysis of 63 cystatins, 32 of which are PhyCys, demonstrate that all PhyCys cluster in a major evolutionary tree branch and support the classification of PhyCys as a new cystatin family. The PhyCys also possess a specific consensus sequence [LVI]-[AGT]-[RKE]-[FY]-[AS]-[VI]-x-[EDQV]-[HYFQ]-N placed on the region corresponding to a predictable amino-terminal α-helix. This sequence can be used to specifically identify PhyCys on protein data banks and to differentiate them from the other members of the superfamily.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Conserved Sequence</subject><subject>cystatins</subject><subject>Cystatins - chemistry</subject><subject>Cystatins - genetics</subject><subject>Cysteine - chemistry</subject><subject>cysteine proteinase inhibitors</subject><subject>Humans</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Phenylalanine - chemistry</subject><subject>Phylogeny</subject><subject>phytocystatins</subject><subject>Plants - chemistry</subject><subject>Plants - genetics</subject><subject>Sequence Homology, Amino Acid</subject><subject>stefins</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kD1PwzAQhi0EKqWwsiFlYks4J7Fjj1XFp5Co-JitxLm0RmlSbAep_x6HVmxMN9xzr957CLmkkFAAflNWlUmolCIBUbAjMqUgeQyZyI_JFACyWApOT8mZc58AlOY8nZCJLKRkjE_J05u3g_aDLduo7Opoud61_Qo79EZHr9iW3vSdW5uti8pN362iZVt2_hedd2YTrhY75wPVuXNy0pStw4vDnJGPu9v3xUP8_HL_uJg_xzoH5mOWNbxKORZMo6S5YDxFCGVS0LKqMa0gryqZsVKkALUQQjaAGVIuKOhGFtmMXO9zt7b_GtB5tTFOYxuKYT84VQCkecFGMNmD2vbOWWzU1obKdqcoqFGeGuWpUZ4a5YWDq0PyUG2w_sMPtsJe7PcY3vs2aJXTBjuNtbGovap781_0D1LyfZ8</recordid><startdate>19981101</startdate><enddate>19981101</enddate><creator>Margis, Rogério</creator><creator>Reis, Emerson M.</creator><creator>Villeret, Vincent</creator><general>Elsevier Inc</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>7X8</scope></search><sort><creationdate>19981101</creationdate><title>Structural and Phylogenetic Relationships among Plant and Animal Cystatins</title><author>Margis, Rogério ; Reis, Emerson M. ; Villeret, Vincent</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c405t-53f6b26e75ce9148562e095520c9bde2b04bb935a8200d8889f0e3e16810cf973</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Conserved Sequence</topic><topic>cystatins</topic><topic>Cystatins - chemistry</topic><topic>Cystatins - genetics</topic><topic>Cysteine - chemistry</topic><topic>cysteine proteinase inhibitors</topic><topic>Humans</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Phenylalanine - chemistry</topic><topic>Phylogeny</topic><topic>phytocystatins</topic><topic>Plants - chemistry</topic><topic>Plants - genetics</topic><topic>Sequence Homology, Amino Acid</topic><topic>stefins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Margis, Rogério</creatorcontrib><creatorcontrib>Reis, Emerson M.</creatorcontrib><creatorcontrib>Villeret, 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>MEDLINE - Academic</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Margis, Rogério</au><au>Reis, Emerson M.</au><au>Villeret, Vincent</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural and Phylogenetic Relationships among Plant and Animal Cystatins</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1998-11-01</date><risdate>1998</risdate><volume>359</volume><issue>1</issue><spage>24</spage><epage>30</epage><pages>24-30</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>The plant cystatins or phytocystatins (PhyCys) are cysteine proteinase inhibitors containing the QxVxG motif and have been placed in the cystatin superfamily of proteins. The primary sequences of PhyCys have a high degree of homology with the members of the cystatin family, but they resemble stefins by the absence of disulfide bonds and cysteine residues. A multialignment and a phylogenetic analysis of 63 cystatins, 32 of which are PhyCys, demonstrate that all PhyCys cluster in a major evolutionary tree branch and support the classification of PhyCys as a new cystatin family. The PhyCys also possess a specific consensus sequence [LVI]-[AGT]-[RKE]-[FY]-[AS]-[VI]-x-[EDQV]-[HYFQ]-N placed on the region corresponding to a predictable amino-terminal α-helix. This sequence can be used to specifically identify PhyCys on protein data banks and to differentiate them from the other members of the superfamily.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>9799556</pmid><doi>10.1006/abbi.1998.0875</doi><tpages>7</tpages></addata></record> |
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| identifier | ISSN: 0003-9861 |
| ispartof | Archives of biochemistry and biophysics, 1998-11, Vol.359 (1), p.24-30 |
| issn | 0003-9861 1096-0384 |
| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Amino Acid Sequence Animals Conserved Sequence cystatins Cystatins - chemistry Cystatins - genetics Cysteine - chemistry cysteine proteinase inhibitors Humans Models, Molecular Molecular Sequence Data Phenylalanine - chemistry Phylogeny phytocystatins Plants - chemistry Plants - genetics Sequence Homology, Amino Acid stefins |
| title | Structural and Phylogenetic Relationships among Plant and Animal Cystatins |
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