Systematic Delineation of a Calmodulin Peptide Interaction
We present a comprehensive profile of amino acid side-chain constraints in a calmodulin (CaM) peptide complex. These data were obtained from the analysis of calmodulin binding to an array of all single substitution analogues as well as N- and C-terminal truncations of the skMLCK derived M13 peptide...
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Veröffentlicht in: | Journal of molecular biology 2004-10, Vol.343 (3), p.559-568 |
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creator | Hultschig, Claus Hecht, Hans-Jürgen Frank, Ronald |
description | We present a comprehensive profile of amino acid side-chain constraints in a calmodulin (CaM) peptide complex. These data were obtained from the analysis of calmodulin binding to an array of all single substitution analogues as well as N- and C-terminal truncations of the skMLCK derived M13 peptide ligand. The experimentally derived binding data were evaluated with respect to the known 3D-structure of the CaM/M13 complex. Besides an almost perfect agreement between the measured affinities and the structural data, the unexpected high-affine Asn5Ala variant of the M13
* peptide described by Montigiani
et al. could be verified. In contrast to other reports our data clearly support the postulate of the minor and major hydrophobic anchors of this calcium dependent interaction. |
doi_str_mv | 10.1016/j.jmb.2004.08.012 |
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* peptide described by Montigiani
et al. could be verified. In contrast to other reports our data clearly support the postulate of the minor and major hydrophobic anchors of this calcium dependent interaction.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/j.jmb.2004.08.012</identifier><identifier>PMID: 15465045</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Calcium - metabolism ; calmodulin ; Calmodulin - chemistry ; Calmodulin - genetics ; Calmodulin - metabolism ; Models, Molecular ; Muscle, Skeletal - metabolism ; Myosin-Light-Chain Kinase - chemistry ; Myosin-Light-Chain Kinase - genetics ; Myosin-Light-Chain Kinase - metabolism ; peptide array ; Peptides - chemistry ; Peptides - genetics ; Peptides - metabolism ; Protein Array Analysis ; Protein Binding ; Protein Conformation ; protein–peptide interaction ; Rabbits ; Sequence Alignment ; SPOT synthesis ; structure activity relationship</subject><ispartof>Journal of molecular biology, 2004-10, Vol.343 (3), p.559-568</ispartof><rights>2004 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c446t-823ec137aad84fc14ccbb7173304d665df80147a348b502251360c89aa0adc8c3</citedby><cites>FETCH-LOGICAL-c446t-823ec137aad84fc14ccbb7173304d665df80147a348b502251360c89aa0adc8c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.jmb.2004.08.012$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15465045$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hultschig, Claus</creatorcontrib><creatorcontrib>Hecht, Hans-Jürgen</creatorcontrib><creatorcontrib>Frank, Ronald</creatorcontrib><title>Systematic Delineation of a Calmodulin Peptide Interaction</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>We present a comprehensive profile of amino acid side-chain constraints in a calmodulin (CaM) peptide complex. These data were obtained from the analysis of calmodulin binding to an array of all single substitution analogues as well as N- and C-terminal truncations of the skMLCK derived M13 peptide ligand. The experimentally derived binding data were evaluated with respect to the known 3D-structure of the CaM/M13 complex. Besides an almost perfect agreement between the measured affinities and the structural data, the unexpected high-affine Asn5Ala variant of the M13
* peptide described by Montigiani
et al. could be verified. In contrast to other reports our data clearly support the postulate of the minor and major hydrophobic anchors of this calcium dependent interaction.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Calcium - metabolism</subject><subject>calmodulin</subject><subject>Calmodulin - chemistry</subject><subject>Calmodulin - genetics</subject><subject>Calmodulin - metabolism</subject><subject>Models, Molecular</subject><subject>Muscle, Skeletal - metabolism</subject><subject>Myosin-Light-Chain Kinase - chemistry</subject><subject>Myosin-Light-Chain Kinase - genetics</subject><subject>Myosin-Light-Chain Kinase - metabolism</subject><subject>peptide array</subject><subject>Peptides - chemistry</subject><subject>Peptides - genetics</subject><subject>Peptides - metabolism</subject><subject>Protein Array Analysis</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>protein–peptide interaction</subject><subject>Rabbits</subject><subject>Sequence Alignment</subject><subject>SPOT synthesis</subject><subject>structure activity relationship</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>eNqFkE1LAzEQhoMotlZ_gBfZk7ddJ5uPTfUk9atQUFDPIZvMQsp-1M2u0H9vSgve9DTD8Lwvw0PIJYWMApU362zdlFkOwDNQGdD8iEwpqHmqJFPHZAqQ52mumJyQsxDWACAYV6dkQgWXAriYktv3bRiwMYO3yQPWvsW4dm3SVYlJFqZuOjfGa_KGm8E7TJbtgL2xO-acnFSmDnhxmDPy-fT4sXhJV6_Py8X9KrWcyyFVOUNLWWGMU7yylFtblgUtGAPupBSuUkB5YeJnpYgPC8okWDU3BoyzyrIZud73bvrua8Qw6MYHi3VtWuzGoKWcc0YF_AvSQiih1A6ke9D2XQg9VnrT-8b0W01B78zqtY5m9c6sBqWj2Zi5OpSPZYPuN3FQGYG7PYDRxbfHXgfrsbXofI920K7zf9T_AK_lh70</recordid><startdate>20041022</startdate><enddate>20041022</enddate><creator>Hultschig, Claus</creator><creator>Hecht, Hans-Jürgen</creator><creator>Frank, Ronald</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>7QP</scope><scope>7X8</scope></search><sort><creationdate>20041022</creationdate><title>Systematic Delineation of a Calmodulin Peptide Interaction</title><author>Hultschig, Claus ; Hecht, Hans-Jürgen ; Frank, Ronald</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c446t-823ec137aad84fc14ccbb7173304d665df80147a348b502251360c89aa0adc8c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Calcium - metabolism</topic><topic>calmodulin</topic><topic>Calmodulin - chemistry</topic><topic>Calmodulin - genetics</topic><topic>Calmodulin - metabolism</topic><topic>Models, Molecular</topic><topic>Muscle, Skeletal - metabolism</topic><topic>Myosin-Light-Chain Kinase - chemistry</topic><topic>Myosin-Light-Chain Kinase - genetics</topic><topic>Myosin-Light-Chain Kinase - metabolism</topic><topic>peptide array</topic><topic>Peptides - chemistry</topic><topic>Peptides - genetics</topic><topic>Peptides - metabolism</topic><topic>Protein Array Analysis</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>protein–peptide interaction</topic><topic>Rabbits</topic><topic>Sequence Alignment</topic><topic>SPOT synthesis</topic><topic>structure activity relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hultschig, Claus</creatorcontrib><creatorcontrib>Hecht, Hans-Jürgen</creatorcontrib><creatorcontrib>Frank, Ronald</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue 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>Hultschig, Claus</au><au>Hecht, Hans-Jürgen</au><au>Frank, Ronald</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Systematic Delineation of a Calmodulin Peptide Interaction</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>2004-10-22</date><risdate>2004</risdate><volume>343</volume><issue>3</issue><spage>559</spage><epage>568</epage><pages>559-568</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><abstract>We present a comprehensive profile of amino acid side-chain constraints in a calmodulin (CaM) peptide complex. 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* peptide described by Montigiani
et al. could be verified. In contrast to other reports our data clearly support the postulate of the minor and major hydrophobic anchors of this calcium dependent interaction.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>15465045</pmid><doi>10.1016/j.jmb.2004.08.012</doi><tpages>10</tpages></addata></record> |
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subjects | Amino Acid Sequence Animals Calcium - metabolism calmodulin Calmodulin - chemistry Calmodulin - genetics Calmodulin - metabolism Models, Molecular Muscle, Skeletal - metabolism Myosin-Light-Chain Kinase - chemistry Myosin-Light-Chain Kinase - genetics Myosin-Light-Chain Kinase - metabolism peptide array Peptides - chemistry Peptides - genetics Peptides - metabolism Protein Array Analysis Protein Binding Protein Conformation protein–peptide interaction Rabbits Sequence Alignment SPOT synthesis structure activity relationship |
title | Systematic Delineation of a Calmodulin Peptide Interaction |
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