Structure and dynamics of the human muscle LIM protein
The family of cysteine rich proteins (CRP) comprises three closely homologous members that have been reported to interact with α-actinin. Muscular LIM protein (MLP/CRP3), the skeletal muscle variant, was originally discovered as a positive regulator of myogenesis and is suggested to be part of the s...
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Veröffentlicht in: | FEBS letters 2009-03, Vol.583 (6), p.1017-1022 |
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creator | Schallus, Thomas Fehér, Krisztina Ulrich, Anne S. Stier, Gunter Muhle-Goll, Claudia |
description | The family of cysteine rich proteins (CRP) comprises three closely homologous members that have been reported to interact with α-actinin. Muscular LIM protein (MLP/CRP3), the skeletal muscle variant, was originally discovered as a positive regulator of myogenesis and is suggested to be part of the stretch sensor of the myofibril through its interaction with telethonin (T-Cap). We determined the structure of both LIM domains of human MLP by nuclear magnetic resonance spectroscopy. We confirm by
15N relaxation measurements that both LIM domains act as independent units and that the adjacent linker regions are fully flexible. With the published structures of CRP1 and CRP2, the complete family has now been structurally characterized. |
doi_str_mv | 10.1016/j.febslet.2009.02.021 |
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15N relaxation measurements that both LIM domains act as independent units and that the adjacent linker regions are fully flexible. With the published structures of CRP1 and CRP2, the complete family has now been structurally characterized.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2009.02.021</identifier><identifier>PMID: 19230835</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Adaptor Proteins, Signal Transducing ; Animals ; Avian Proteins - chemistry ; C-terminal LIM domain of MLP ; Carrier Proteins - chemistry ; CRP ; Cysteine rich protein ; DNA-Binding Proteins - chemistry ; Eye Proteins - chemistry ; heteronuclear NOE ; heteronuclear single quantum coherence ; hetNOE ; Homeodomain Proteins - chemistry ; HSQC ; Humans ; LIM Domain Proteins ; LIM-Homeodomain Proteins ; LIM1 ; LIM2 ; Membrane Proteins ; MLP ; Models, Molecular ; Muscle Proteins - chemistry ; Muscle Proteins - genetics ; Muscle Proteins - physiology ; muscular LIM protein ; N-terminal LIM domain of MLP ; NMR ; NOE ; NOESY ; Nuclear Magnetic Resonance, Biomolecular ; nuclear overhauser effect ; nuclear overhauser enhancement spectroscopy ; Protein Folding ; Protein Structure, Tertiary ; RMSD ; root mean square deviation ; Telethonin ; Thermodynamics ; Transcription Factors ; α-Actinin</subject><ispartof>FEBS letters, 2009-03, Vol.583 (6), p.1017-1022</ispartof><rights>2009 Federation of European Biochemical Societies</rights><rights>FEBS Letters 583 (2009) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4757-b413bd0037d329c7f4a22351b16bb3005f3f5519ca5d715600b1b2a70d8cc0df3</citedby><cites>FETCH-LOGICAL-c4757-b413bd0037d329c7f4a22351b16bb3005f3f5519ca5d715600b1b2a70d8cc0df3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2009.02.021$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579309001197$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3536,27903,27904,45553,45554,46387,46811,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19230835$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schallus, Thomas</creatorcontrib><creatorcontrib>Fehér, Krisztina</creatorcontrib><creatorcontrib>Ulrich, Anne S.</creatorcontrib><creatorcontrib>Stier, Gunter</creatorcontrib><creatorcontrib>Muhle-Goll, Claudia</creatorcontrib><title>Structure and dynamics of the human muscle LIM protein</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The family of cysteine rich proteins (CRP) comprises three closely homologous members that have been reported to interact with α-actinin. Muscular LIM protein (MLP/CRP3), the skeletal muscle variant, was originally discovered as a positive regulator of myogenesis and is suggested to be part of the stretch sensor of the myofibril through its interaction with telethonin (T-Cap). We determined the structure of both LIM domains of human MLP by nuclear magnetic resonance spectroscopy. We confirm by
15N relaxation measurements that both LIM domains act as independent units and that the adjacent linker regions are fully flexible. With the published structures of CRP1 and CRP2, the complete family has now been structurally characterized.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Animals</subject><subject>Avian Proteins - chemistry</subject><subject>C-terminal LIM domain of MLP</subject><subject>Carrier Proteins - chemistry</subject><subject>CRP</subject><subject>Cysteine rich protein</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>Eye Proteins - chemistry</subject><subject>heteronuclear NOE</subject><subject>heteronuclear single quantum coherence</subject><subject>hetNOE</subject><subject>Homeodomain Proteins - chemistry</subject><subject>HSQC</subject><subject>Humans</subject><subject>LIM Domain Proteins</subject><subject>LIM-Homeodomain Proteins</subject><subject>LIM1</subject><subject>LIM2</subject><subject>Membrane Proteins</subject><subject>MLP</subject><subject>Models, Molecular</subject><subject>Muscle Proteins - chemistry</subject><subject>Muscle Proteins - genetics</subject><subject>Muscle Proteins - physiology</subject><subject>muscular LIM protein</subject><subject>N-terminal LIM domain of MLP</subject><subject>NMR</subject><subject>NOE</subject><subject>NOESY</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>nuclear overhauser effect</subject><subject>nuclear overhauser enhancement spectroscopy</subject><subject>Protein Folding</subject><subject>Protein Structure, Tertiary</subject><subject>RMSD</subject><subject>root mean square deviation</subject><subject>Telethonin</subject><subject>Thermodynamics</subject><subject>Transcription Factors</subject><subject>α-Actinin</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE2LFDEQhoMo7rj6E5Q-eeuxKul0OifRZdddGPGweg75qGYz9MeadK_MvzfjDHhUKKgqeOt9i4extwhbBGw_7Lc9uTzQsuUAegu8FD5jG-yUqEXTds_ZBgCbWiotLtirnPdQ9g71S3aBmgvohNyw9n5Jq1_WRJWdQhUOkx2jz9XcV8sDVQ_raKdqXLMfqNrdfa0e07xQnF6zF70dMr0590v24-b6-9Vtvfv25e7q0672jZKqdg0KFwCECoJrr_rGci4kOmydEwCyF72UqL2VQaFsARw6bhWEznsIvbhk70--JffnSnkxY8yehsFONK_ZtAq45loVoTwJfZpzTtSbxxRHmw4GwRyBmb05AzNHYAZ4KSx3784Bqxsp_L06EyqC25PgVxzo8H-u5ub6M78_0j_CB10m_PPjx5MVFWJPkZLJPtLkKcREfjFhjv_49jfC_JKl</recordid><startdate>20090318</startdate><enddate>20090318</enddate><creator>Schallus, Thomas</creator><creator>Fehér, Krisztina</creator><creator>Ulrich, Anne S.</creator><creator>Stier, Gunter</creator><creator>Muhle-Goll, Claudia</creator><general>Elsevier B.V</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>20090318</creationdate><title>Structure and dynamics of the human muscle LIM protein</title><author>Schallus, Thomas ; Fehér, Krisztina ; Ulrich, Anne S. ; Stier, Gunter ; Muhle-Goll, Claudia</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4757-b413bd0037d329c7f4a22351b16bb3005f3f5519ca5d715600b1b2a70d8cc0df3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Adaptor Proteins, Signal Transducing</topic><topic>Animals</topic><topic>Avian Proteins - chemistry</topic><topic>C-terminal LIM domain of MLP</topic><topic>Carrier Proteins - chemistry</topic><topic>CRP</topic><topic>Cysteine rich protein</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>Eye Proteins - chemistry</topic><topic>heteronuclear NOE</topic><topic>heteronuclear single quantum coherence</topic><topic>hetNOE</topic><topic>Homeodomain Proteins - chemistry</topic><topic>HSQC</topic><topic>Humans</topic><topic>LIM Domain Proteins</topic><topic>LIM-Homeodomain Proteins</topic><topic>LIM1</topic><topic>LIM2</topic><topic>Membrane Proteins</topic><topic>MLP</topic><topic>Models, Molecular</topic><topic>Muscle Proteins - chemistry</topic><topic>Muscle Proteins - genetics</topic><topic>Muscle Proteins - physiology</topic><topic>muscular LIM protein</topic><topic>N-terminal LIM domain of MLP</topic><topic>NMR</topic><topic>NOE</topic><topic>NOESY</topic><topic>Nuclear Magnetic Resonance, Biomolecular</topic><topic>nuclear overhauser effect</topic><topic>nuclear overhauser enhancement spectroscopy</topic><topic>Protein Folding</topic><topic>Protein Structure, Tertiary</topic><topic>RMSD</topic><topic>root mean square deviation</topic><topic>Telethonin</topic><topic>Thermodynamics</topic><topic>Transcription Factors</topic><topic>α-Actinin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schallus, Thomas</creatorcontrib><creatorcontrib>Fehér, Krisztina</creatorcontrib><creatorcontrib>Ulrich, Anne S.</creatorcontrib><creatorcontrib>Stier, Gunter</creatorcontrib><creatorcontrib>Muhle-Goll, Claudia</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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schallus, Thomas</au><au>Fehér, Krisztina</au><au>Ulrich, Anne S.</au><au>Stier, Gunter</au><au>Muhle-Goll, Claudia</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure and dynamics of the human muscle LIM protein</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2009-03-18</date><risdate>2009</risdate><volume>583</volume><issue>6</issue><spage>1017</spage><epage>1022</epage><pages>1017-1022</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The family of cysteine rich proteins (CRP) comprises three closely homologous members that have been reported to interact with α-actinin. Muscular LIM protein (MLP/CRP3), the skeletal muscle variant, was originally discovered as a positive regulator of myogenesis and is suggested to be part of the stretch sensor of the myofibril through its interaction with telethonin (T-Cap). We determined the structure of both LIM domains of human MLP by nuclear magnetic resonance spectroscopy. We confirm by
15N relaxation measurements that both LIM domains act as independent units and that the adjacent linker regions are fully flexible. With the published structures of CRP1 and CRP2, the complete family has now been structurally characterized.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>19230835</pmid><doi>10.1016/j.febslet.2009.02.021</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Adaptor Proteins, Signal Transducing Animals Avian Proteins - chemistry C-terminal LIM domain of MLP Carrier Proteins - chemistry CRP Cysteine rich protein DNA-Binding Proteins - chemistry Eye Proteins - chemistry heteronuclear NOE heteronuclear single quantum coherence hetNOE Homeodomain Proteins - chemistry HSQC Humans LIM Domain Proteins LIM-Homeodomain Proteins LIM1 LIM2 Membrane Proteins MLP Models, Molecular Muscle Proteins - chemistry Muscle Proteins - genetics Muscle Proteins - physiology muscular LIM protein N-terminal LIM domain of MLP NMR NOE NOESY Nuclear Magnetic Resonance, Biomolecular nuclear overhauser effect nuclear overhauser enhancement spectroscopy Protein Folding Protein Structure, Tertiary RMSD root mean square deviation Telethonin Thermodynamics Transcription Factors α-Actinin |
title | Structure and dynamics of the human muscle LIM protein |
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