{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,23]],"date-time":"2026-06-23T15:40:08Z","timestamp":1782229208009,"version":"3.54.5"},"reference-count":38,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"5074","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Science"],"published-print":{"date-parts":[[1992,8,28]]},"abstract":"<jats:p>\n            The crystal structure of calcium-bound calmodulin (Ca\n            <jats:sup>2+<\/jats:sup>\n            -CaM) bound to a peptide analog of the CaM-binding region of chicken smooth muscle myosin light chain kinase has been determined and refined to a resolution of 2.4 angstroms (\u00c5). The structure is compact and has the shape of an ellipsoid (axial ratio \u223c2:1). The bound CaM forms a tunnel diagonal to its long axis that engulfs the helical peptide, with the hydrophobic regions of CaM melded into a single area that closely covers the hydrophobic side of the peptide. There is a remarkably high pseudo-twofold symmetry between the closely associated domains. The central helix of the native CaM is unwound and expanded into a bend between residues 73 and 77. About 185 contacts (&lt;4 \u00c5) are formed between CaM and the peptide, with van der Waals contacts comprising \u223c80% of this total.\n          <\/jats:p>","DOI":"10.1126\/science.1519061","type":"journal-article","created":{"date-parts":[[2006,10,5]],"date-time":"2006-10-05T23:03:06Z","timestamp":1160089386000},"page":"1251-1255","source":"Crossref","is-referenced-by-count":842,"title":["Target Enzyme Recognition by Calmodulin: 2.4 \u00c5 Structure of a Calmodulin-Peptide Complex"],"prefix":"10.1126","volume":"257","author":[{"given":"William E.","family":"Meador","sequence":"first","affiliation":[{"name":"Howard Hughes Medical Institute and Department of Biochemistry, Baylor College of Medicine, Houston, TX 77030."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anthony R.","family":"Means","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, Duke University Medical Center, Durham, NC 27710."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Florante A.","family":"Quiocho","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute and Department of Biochemistry, Baylor College of Medicine, Houston, TX 77030."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"221","reference":[{"key":"e_1_2_1_1_1","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/0022-2836(88)90608-0","volume":"204","year":"1988","unstructured":"BABU, Y.S., STRUCTURE OF CALMODULIN REFINED AT 2.2 A RESOLUTION, JOURNAL OF MOLECULAR BIOLOGY 204: 191 (1988).","journal-title":"JOURNAL OF MOLECULAR BIOLOGY"},{"key":"e_1_2_1_2_1","doi-asserted-by":"crossref","first-page":"3024","DOI":"10.1016\/S0021-9258(19)50689-5","volume":"267","year":"1992","unstructured":"BAGCHI, I.C., IDENTIFICATION OF AMINO-ACIDS ESSENTIAL FOR CALMODULIN BINDING AND ACTIVATION OF SMOOTH-MUSCLE MYOSIN LIGHT CHAIN KINASE, JOURNAL OF BIOLOGICAL CHEMISTRY 267: 3024 (1992).","journal-title":"JOURNAL OF BIOLOGICAL CHEMISTRY"},{"key":"e_1_2_1_3_1","first-page":"3187","volume":"82","year":"1985","unstructured":"BLUMENTHAL, D.K., IDENTIFICATION OF THE CALMODULIN-BINDING DOMAIN OF SKELETAL-MUSCLE MYOSIN LIGHT CHAIN KINASE, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 82: 3187 (1985).","journal-title":"PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA"},{"key":"e_1_2_1_4_1","doi-asserted-by":"crossref","unstructured":"Brunger A. T. X-PLOR Version 2.1: A System for Crystallography and NMR (1990).","DOI":"10.1038\/nprot.2007.406"},{"key":"e_1_2_1_5_1","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/0263-7855(87)80010-3","volume":"5","year":"1987","unstructured":"CARSON, M, RIBBON MODELS OF MACROMOLECULES, JOURNAL OF MOLECULAR GRAPHICS 5: 103 (1987).","journal-title":"JOURNAL OF MOLECULAR GRAPHICS"},{"key":"e_1_2_1_6_1","doi-asserted-by":"crossref","first-page":"1177","DOI":"10.1016\/0022-2836(92)90324-D","volume":"228","year":"1992","unstructured":"Chattopadhyaya, R., Journal of Molecular Biology 228: 1177 (1992).","journal-title":"Journal of Molecular Biology"},{"key":"e_1_2_1_7_1","doi-asserted-by":"crossref","first-page":"2527","DOI":"10.1016\/S0021-9258(18)89584-9","volume":"260","year":"1985","unstructured":"COX, J.A., THE INTERACTION OF CALMODULIN WITH AMPHIPHILIC PEPTIDES, JOURNAL OF BIOLOGICAL CHEMISTRY 260: 2527 (1985).","journal-title":"JOURNAL OF BIOLOGICAL CHEMISTRY"},{"key":"e_1_2_1_8_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.3037704"},{"key":"e_1_2_1_9_1","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1021\/bi00403a011","volume":"27","year":"1988","unstructured":"HEIDORN, D.B., COMPARISON OF THE CRYSTAL AND SOLUTION STRUCTURES OF CALMODULIN AND TROPONIN-C, BIOCHEMISTRY 27: 909 (1988).","journal-title":"BIOCHEMISTRY"},{"key":"e_1_2_1_10_1","doi-asserted-by":"crossref","first-page":"5498","DOI":"10.1021\/bi00236a024","volume":"30","year":"1991","unstructured":"IKURA, M, TRIPLE-RESONANCE MULTIDIMENSIONAL NMR-STUDY OF CALMODULIN COMPLEXED WITH THE BINDING DOMAIN OF SKELETAL-MUSCLE MYOSIN LIGHT-CHAIN KINASE - INDICATION OF A CONFORMATIONAL CHANGE IN THE CENTRAL HELIX, BIOCHEMISTRY 30: 5498 (1991).","journal-title":"BIOCHEMISTRY"},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1585175"},{"key":"e_1_2_1_12_1","doi-asserted-by":"crossref","first-page":"3498","DOI":"10.1021\/bi00228a021","volume":"30","year":"1991","unstructured":"ITO, M, DEFINITION OF THE INHIBITORY DOMAIN OF SMOOTH-MUSCLE MYOSIN LIGHT CHAIN KINASE BY SITE-DIRECTED MUTAGENESIS, BIOCHEMISTRY 30: 3498 (1991).","journal-title":"BIOCHEMISTRY"},{"key":"e_1_2_1_13_1","doi-asserted-by":"crossref","first-page":"6247","DOI":"10.1021\/bi00239a024","volume":"30","year":"1991","unstructured":"KATAOKA, M, SMALL-ANGLE X-RAY-SCATTERING STUDY OF CALMODULIN BOUND TO 2 PEPTIDES CORRESPONDING TO PARTS OF THE CALMODULIN-BINDING DOMAIN OF THE PLASMA-MEMBRANE CA2+ PUMP, BIOCHEMISTRY 30: 6247 (1991).","journal-title":"BIOCHEMISTRY"},{"key":"e_1_2_1_14_1","doi-asserted-by":"crossref","first-page":"2542","DOI":"10.1016\/S0021-9258(18)61538-8","volume":"262","year":"1987","unstructured":"KEMP, B.E., THE CALMODULIN BINDING DOMAIN OF CHICKEN SMOOTH-MUSCLE MYOSIN LIGHT CHAIN KINASE CONTAINS A PSEUDOSUBSTRATE SEQUENCE, JOURNAL OF BIOLOGICAL CHEMISTRY 262: 2542 (1987).","journal-title":"JOURNAL OF BIOLOGICAL CHEMISTRY"},{"key":"e_1_2_1_15_1","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/S0065-3233(08)60470-2","volume":"35","year":"1982","unstructured":"KLEE, C.B., CALMODULIN, ADVANCES IN PROTEIN CHEMISTRY 35: 213 (1982).","journal-title":"ADVANCES IN PROTEIN CHEMISTRY"},{"key":"e_1_2_1_16_1","doi-asserted-by":"crossref","first-page":"4930","DOI":"10.1016\/S0021-9258(18)42920-1","volume":"267","year":"1992","unstructured":"LEACHMAN, S.A., BIOCHEMICAL-PROPERTIES OF CHIMERIC SKELETAL AND SMOOTH-MUSCLE MYOSIN LIGHT CHAIN KINASES, JOURNAL OF BIOLOGICAL CHEMISTRY 267: 4930 (1992).","journal-title":"JOURNAL OF BIOLOGICAL CHEMISTRY"},{"key":"e_1_2_1_17_1","doi-asserted-by":"crossref","first-page":"1458","DOI":"10.1021\/bi00354a041","volume":"25","year":"1986","unstructured":"LUKAS, T.J., CALMODULIN BINDING DOMAINS - CHARACTERIZATION OF A PHOSPHORYLATION AND CALMODULIN BINDING-SITE FROM MYOSIN LIGHT CHAIN KINASE, BIOCHEMISTRY 25: 1458 (1986).","journal-title":"BIOCHEMISTRY"},{"key":"e_1_2_1_18_1","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1101\/SQB.1988.053.01.024","volume":"53","year":"1988","unstructured":"Lukas, T. J., Cold Spring Harbor Symposia on Quantitative Biology 53: 185 (1988).","journal-title":"Cold Spring Harbor Symposia on Quantitative Biology"},{"key":"e_1_2_1_19_1","doi-asserted-by":"crossref","first-page":"2979","DOI":"10.1021\/bi00333a026","volume":"24","year":"1985","unstructured":"MCDOWELL, L, PROBABLE ROLE OF AMPHIPHILICITY IN THE BINDING OF MASTOPARAN TO CALMODULIN, BIOCHEMISTRY 24: 2979 (1985).","journal-title":"BIOCHEMISTRY"},{"key":"e_1_2_1_20_1","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/0163-7258(91)90017-G","volume":"50","year":"1991","unstructured":"MEANS, A. R., PHARMACOLOGY & THERAPEUTICS 50: 255 (1991).","journal-title":"PHARMACOLOGY & THERAPEUTICS"},{"key":"e_1_2_1_21_1","doi-asserted-by":"crossref","first-page":"14571","DOI":"10.1016\/S0021-9258(18)71717-1","volume":"264","year":"1989","unstructured":"ONEIL, K.T., PHOTOLABELING OF CALMODULIN WITH BASIC, AMPHIPHILIC ALPHA-HELICAL PEPTIDES CONTAINING PARA-BENZOYLPHENYLALANINE, JOURNAL OF BIOLOGICAL CHEMISTRY 264: 14571 (1989).","journal-title":"JOURNAL OF BIOLOGICAL CHEMISTRY"},{"key":"e_1_2_1_22_1","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/0968-0004(90)90177-D","volume":"15","year":"1990","unstructured":"ONEIL, K.T., HOW CALMODULIN BINDS ITS TARGETS - SEQUENCE INDEPENDENT RECOGNITION OF AMPHIPHILIC ALPHA-HELICES, TRENDS IN BIOCHEMICAL SCIENCES 15: 59 (1990).","journal-title":"TRENDS IN BIOCHEMICAL SCIENCES"},{"key":"e_1_2_1_23_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.3406746"},{"key":"e_1_2_1_24_1","doi-asserted-by":"crossref","first-page":"12175","DOI":"10.1016\/S0021-9258(18)37733-0","volume":"263","year":"1988","unstructured":"PERSECHINI, A, THE CENTRAL HELIX OF CALMODULIN FUNCTIONS AS A FLEXIBLE TETHER, JOURNAL OF BIOLOGICAL CHEMISTRY 263: 12175 (1988).","journal-title":"JOURNAL OF BIOLOGICAL CHEMISTRY"},{"key":"e_1_2_1_25_1","doi-asserted-by":"crossref","first-page":"8052","DOI":"10.1016\/S0021-9258(18)83149-0","volume":"264","year":"1989","unstructured":"PERSECHINI, A, THE EFFECTS OF DELETIONS IN THE CENTRAL HELIX OF CALMODULIN ON ENZYME ACTIVATION AND PEPTIDE BINDING, JOURNAL OF BIOLOGICAL CHEMISTRY 264: 8052 (1989).","journal-title":"JOURNAL OF BIOLOGICAL CHEMISTRY"},{"key":"e_1_2_1_26_1","first-page":"501","volume":"12","year":"1988","unstructured":"PERSECHINI, A, J CARDIOVASC PHARM 12: 501 (1988).","journal-title":"J CARDIOVASC PHARM"},{"key":"e_1_2_1_27_1","doi-asserted-by":"crossref","first-page":"11242","DOI":"10.1016\/S0021-9258(18)37948-1","volume":"263","year":"1988","unstructured":"PUTKEY, J.A., FUNCTIONAL-SIGNIFICANCE OF THE CENTRAL HELIX IN CALMODULIN, JOURNAL OF BIOLOGICAL CHEMISTRY 263: 11242 (1988).","journal-title":"JOURNAL OF BIOLOGICAL CHEMISTRY"},{"key":"e_1_2_1_28_1","doi-asserted-by":"crossref","first-page":"1443","DOI":"10.1021\/bi00120a022","volume":"31","year":"1992","unstructured":"ROTH, S.M., CHARACTERIZATION OF THE SECONDARY STRUCTURE OF CALMODULIN IN COMPLEX WITH A CALMODULIN-BINDING DOMAIN PEPTIDE, BIOCHEMISTRY 31: 1443 (1992).","journal-title":"BIOCHEMISTRY"},{"key":"e_1_2_1_29_1","first-page":"224","volume":"6","year":"1988","unstructured":"SACK, J, JOURNAL OF MOLECULAR GRAPHICS 6: 224 (1988).","journal-title":"JOURNAL OF MOLECULAR GRAPHICS"},{"key":"e_1_2_1_30_1","first-page":"360","year":"1987","unstructured":"Seeholzer, S. H., Calcium-Binding Proteins in Health and Disease: 360 (1987).","journal-title":"Calcium-Binding Proteins in Health and Disease"},{"key":"e_1_2_1_31_1","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1083\/jcb.111.3.1107","volume":"111","year":"1990","unstructured":"SHOEMAKER, M.O., USE OF DNA-SEQUENCE AND MUTANT ANALYSES AND ANTISENSE OLIGODEOXYNUCLEOTIDES TO EXAMINE THE MOLECULAR-BASIS OF NONMUSCLE MYOSIN LIGHT CHAIN KINASE AUTOINHIBITION, CALMODULIN RECOGNITION, AND ACTIVITY, JOURNAL OF CELL BIOLOGY 111: 1107 (1990).","journal-title":"JOURNAL OF CELL BIOLOGY"},{"key":"e_1_2_1_32_1","unstructured":"STEIGEMANN W THESIS TU MUNCHEN (1974)."},{"key":"e_1_2_1_33_1","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1002\/prot.340070305","volume":"7","year":"1990","unstructured":"STRYNADKA, N. C. J., PROTEINS-STRUCTURE FUNCTION AND GENETICS 7: 234 (1990).","journal-title":"PROTEINS-STRUCTURE FUNCTION AND GENETICS"},{"key":"e_1_2_1_34_1","doi-asserted-by":"crossref","first-page":"3452","DOI":"10.1021\/bi00128a020","volume":"31","year":"1992","unstructured":"TOROK, K, EFFECTS OF CALCIUM-BINDING ON THE INTERNAL DYNAMIC PROPERTIES OF BOVINE BRAIN CALMODULIN, STUDIED BY NMR AND OPTICAL SPECTROSCOPY, BIOCHEMISTRY 31: 3452 (1992).","journal-title":"BIOCHEMISTRY"},{"key":"e_1_2_1_35_1","doi-asserted-by":"crossref","first-page":"3750","DOI":"10.1016\/S0021-9258(19)39658-9","volume":"265","year":"1990","unstructured":"VanBerkum, M. F., Journal of Biological Chemistry 265: 3750 (1990).","journal-title":"Journal of Biological Chemistry"},{"key":"e_1_2_1_36_1","doi-asserted-by":"crossref","first-page":"21488","DOI":"10.1016\/S0021-9258(18)54665-2","volume":"266","year":"1991","unstructured":"VANBERKUM, MFA, 3 AMINO-ACID SUBSTITUTIONS IN DOMAIN-I OF CALMODULIN PREVENT THE ACTIVATION OF CHICKEN SMOOTH-MUSCLE MYOSIN LIGHT CHAIN KINASE, JOURNAL OF BIOLOGICAL CHEMISTRY 266: 21488 (1991).","journal-title":"JOURNAL OF BIOLOGICAL CHEMISTRY"},{"key":"e_1_2_1_37_1","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1021\/bi00454a008","volume":"29","year":"1990","unstructured":"VORHERR, T, BIOCHEMISTRY 29: 355 (1990).","journal-title":"BIOCHEMISTRY"},{"key":"e_1_2_1_38_1","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1111\/j.1432-1033.1992.tb16714.x","volume":"204","year":"1992","unstructured":"VORHERR, T, CONSTRUCTION AND MOLECULAR-DYNAMICS SIMULATION OF CALMODULIN IN THE EXTENDED AND IN A BENT CONFORMATION, EUROPEAN JOURNAL OF BIOCHEMISTRY 204: 931 (1992).","journal-title":"EUROPEAN JOURNAL OF BIOCHEMISTRY"}],"container-title":["Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.science.org\/doi\/pdf\/10.1126\/science.1519061","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,1,11]],"date-time":"2024-01-11T10:24:25Z","timestamp":1704968665000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.science.org\/doi\/10.1126\/science.1519061"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1992,8,28]]},"references-count":38,"journal-issue":{"issue":"5074","published-print":{"date-parts":[[1992,8,28]]}},"alternative-id":["10.1126\/science.1519061"],"URL":"https:\/\/doi.org\/10.1126\/science.1519061","relation":{},"ISSN":["0036-8075","1095-9203"],"issn-type":[{"value":"0036-8075","type":"print"},{"value":"1095-9203","type":"electronic"}],"subject":[],"published":{"date-parts":[[1992,8,28]]}}}