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...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Journal of molecular biology 2004-10, Vol.343 (3), p.559-568
Hauptverfasser: Hultschig, Claus, Hecht, Hans-Jürgen, Frank, Ronald
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 568
container_issue 3
container_start_page 559
container_title Journal of molecular biology
container_volume 343
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
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_66943150</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0022283604009799</els_id><sourcerecordid>17585880</sourcerecordid><originalsourceid>FETCH-LOGICAL-c446t-823ec137aad84fc14ccbb7173304d665df80147a348b502251360c89aa0adc8c3</originalsourceid><addsrcrecordid>eNqFkE1LAzEQhoMotlZ_gBfZk7ddJ5uPTfUk9atQUFDPIZvMQsp-1M2u0H9vSgve9DTD8Lwvw0PIJYWMApU362zdlFkOwDNQGdD8iEwpqHmqJFPHZAqQ52mumJyQsxDWACAYV6dkQgWXAriYktv3bRiwMYO3yQPWvsW4dm3SVYlJFqZuOjfGa_KGm8E7TJbtgL2xO-acnFSmDnhxmDPy-fT4sXhJV6_Py8X9KrWcyyFVOUNLWWGMU7yylFtblgUtGAPupBSuUkB5YeJnpYgPC8okWDU3BoyzyrIZud73bvrua8Qw6MYHi3VtWuzGoKWcc0YF_AvSQiih1A6ke9D2XQg9VnrT-8b0W01B78zqtY5m9c6sBqWj2Zi5OpSPZYPuN3FQGYG7PYDRxbfHXgfrsbXofI920K7zf9T_AK_lh70</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17585880</pqid></control><display><type>article</type><title>Systematic Delineation of a Calmodulin Peptide Interaction</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Hultschig, Claus ; Hecht, Hans-Jürgen ; Frank, Ronald</creator><creatorcontrib>Hultschig, Claus ; Hecht, Hans-Jürgen ; Frank, Ronald</creatorcontrib><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><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 &amp; 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. 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.</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>
fulltext fulltext
identifier ISSN: 0022-2836
ispartof Journal of molecular biology, 2004-10, Vol.343 (3), p.559-568
issn 0022-2836
1089-8638
language eng
recordid cdi_proquest_miscellaneous_66943150
source MEDLINE; Elsevier ScienceDirect Journals Complete
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
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T07%3A59%3A31IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Systematic%20Delineation%20of%20a%20Calmodulin%20Peptide%20Interaction&rft.jtitle=Journal%20of%20molecular%20biology&rft.au=Hultschig,%20Claus&rft.date=2004-10-22&rft.volume=343&rft.issue=3&rft.spage=559&rft.epage=568&rft.pages=559-568&rft.issn=0022-2836&rft.eissn=1089-8638&rft_id=info:doi/10.1016/j.jmb.2004.08.012&rft_dat=%3Cproquest_cross%3E17585880%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=17585880&rft_id=info:pmid/15465045&rft_els_id=S0022283604009799&rfr_iscdi=true