Solution structure of calcium-free calmodulin
The three-dimensional structure of calmodulin in the absence of Ca 2+ has been determined by three- and four-dimensional heteronuclear NMR experiments, including ROE, isotope-filtering combined with reverse labelling, and measurement of more than 700 three-bond J -couplings. In analogy with the Ca 2...
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| Veröffentlicht in: | Nature Structural Biology 1995-09, Vol.2 (9), p.768-776 |
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| container_title | Nature Structural Biology |
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| creator | Kuboniwa, Hitoshi Tjandra, Nico Grzesiek, Stephan Ren, Hao Klee, Claude B. Bax, Ad |
| description | The three-dimensional structure of calmodulin in the absence of Ca
2+
has been determined by three- and four-dimensional heteronuclear NMR experiments, including ROE, isotope-filtering combined with reverse labelling, and measurement of more than 700 three-bond
J
-couplings. In analogy with the Ca
2+
-ligated state of this protein, it consists of two small globular domains separated by a flexible linker, with no stable, direct contacts between the two domains. In the absence of Ca
2+
, the four helices in each of the two globular domains form a highly twisted bundle, capped by a short anti-parallel β-sheet. This arrangement is qualitatively similar to that observed in the crystal structure of the Ca
2+
-free N-terminal domain of troponin C. |
| doi_str_mv | 10.1038/nsb0995-768 |
| format | Article |
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2+
has been determined by three- and four-dimensional heteronuclear NMR experiments, including ROE, isotope-filtering combined with reverse labelling, and measurement of more than 700 three-bond
J
-couplings. In analogy with the Ca
2+
-ligated state of this protein, it consists of two small globular domains separated by a flexible linker, with no stable, direct contacts between the two domains. In the absence of Ca
2+
, the four helices in each of the two globular domains form a highly twisted bundle, capped by a short anti-parallel β-sheet. This arrangement is qualitatively similar to that observed in the crystal structure of the Ca
2+
-free N-terminal domain of troponin C.</description><identifier>ISSN: 1072-8368</identifier><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/nsb0995-768</identifier><identifier>PMID: 7552748</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Animals ; Biochemistry ; Biological Microscopy ; Calcium - chemistry ; Calcium - metabolism ; Calmodulin - chemistry ; Calmodulin - metabolism ; Carbon Isotopes ; Isotope Labeling ; Life Sciences ; Magnetic Resonance Spectroscopy - methods ; Membrane Biology ; Phenylalanine - chemistry ; Protein Conformation ; Protein Structure ; Solutions</subject><ispartof>Nature Structural Biology, 1995-09, Vol.2 (9), p.768-776</ispartof><rights>Springer Nature Limited 1995</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c321t-6bb05a01b65878fffb34661294d6f0f7e4ec86c0d790a785d0cc746b6792f683</citedby><cites>FETCH-LOGICAL-c321t-6bb05a01b65878fffb34661294d6f0f7e4ec86c0d790a785d0cc746b6792f683</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/nsb0995-768$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nsb0995-768$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7552748$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kuboniwa, Hitoshi</creatorcontrib><creatorcontrib>Tjandra, Nico</creatorcontrib><creatorcontrib>Grzesiek, Stephan</creatorcontrib><creatorcontrib>Ren, Hao</creatorcontrib><creatorcontrib>Klee, Claude B.</creatorcontrib><creatorcontrib>Bax, Ad</creatorcontrib><title>Solution structure of calcium-free calmodulin</title><title>Nature Structural Biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Biol</addtitle><description>The three-dimensional structure of calmodulin in the absence of Ca
2+
has been determined by three- and four-dimensional heteronuclear NMR experiments, including ROE, isotope-filtering combined with reverse labelling, and measurement of more than 700 three-bond
J
-couplings. In analogy with the Ca
2+
-ligated state of this protein, it consists of two small globular domains separated by a flexible linker, with no stable, direct contacts between the two domains. In the absence of Ca
2+
, the four helices in each of the two globular domains form a highly twisted bundle, capped by a short anti-parallel β-sheet. This arrangement is qualitatively similar to that observed in the crystal structure of the Ca
2+
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2+
has been determined by three- and four-dimensional heteronuclear NMR experiments, including ROE, isotope-filtering combined with reverse labelling, and measurement of more than 700 three-bond
J
-couplings. In analogy with the Ca
2+
-ligated state of this protein, it consists of two small globular domains separated by a flexible linker, with no stable, direct contacts between the two domains. In the absence of Ca
2+
, the four helices in each of the two globular domains form a highly twisted bundle, capped by a short anti-parallel β-sheet. This arrangement is qualitatively similar to that observed in the crystal structure of the Ca
2+
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| ispartof | Nature Structural Biology, 1995-09, Vol.2 (9), p.768-776 |
| issn | 1072-8368 1545-9993 1545-9985 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77563737 |
| source | MEDLINE; SpringerLink Journals; Nature Journals Online |
| subjects | Animals Biochemistry Biological Microscopy Calcium - chemistry Calcium - metabolism Calmodulin - chemistry Calmodulin - metabolism Carbon Isotopes Isotope Labeling Life Sciences Magnetic Resonance Spectroscopy - methods Membrane Biology Phenylalanine - chemistry Protein Conformation Protein Structure Solutions |
| title | Solution structure of calcium-free calmodulin |
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