pubmed-article:4065103 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:4065103 | lifeskim:mentions | umls-concept:C0001271 | lld:lifeskim |
pubmed-article:4065103 | lifeskim:mentions | umls-concept:C0011519 | lld:lifeskim |
pubmed-article:4065103 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:4065103 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:4065103 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
pubmed-article:4065103 | lifeskim:mentions | umls-concept:C0450363 | lld:lifeskim |
pubmed-article:4065103 | pubmed:issue | 8 | lld:pubmed |
pubmed-article:4065103 | pubmed:dateCreated | 1986-1-6 | lld:pubmed |
pubmed-article:4065103 | pubmed:abstractText | The shape of an actin subunit has been derived from an improved 6 A map of the complex of rabbit skeletal muscle actin and bovine pancreatic DNase I obtained by X-ray crystallographic methods. The three-dimensional structure of DNase I determined independently at 2.5 A resolution was compared with the DNase I electron density in the actin:DNase map. The two structures are very similar at 6 A resolution thus leading to an unambiguous identification of actin as well as DNase I electron density. Furthermore the correct hand of the actin structure is determined from the DNase I atomic structure. The resolution of the actin structure was extended to 4.5 A by using a single heavy-atom derivative and the knowledge of the atomic coordinates of DNase I. The dimensions of an actin subunit are 67 A X 40 A X 37 A. It consists of a small and a large domain, the small domain containing the N terminus. Actin is an alpha,beta-protein with a beta-pleated sheet in each domain. These sheets are surrounded by several alpha-helices, comprising at least 40% of the structure. The phosphate peak of the adenine nucleotide is located between the two domains. The complex of actin and DNase I as found in solution (i.e., the actin:DNase I contacts which do not depend on crystal packing) was deduced from a comparison of monoclinic with orthorhombic crystals. Residues 44-46, 51, 52, 60-62 of DNase I are close to a loop region in the small domain of actin. At a distance of approximately 15 A there is a second contact in the large domain in which Glu13 of DNase I is involved. A possible binding region for myosin is discussed. | lld:pubmed |
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pubmed-article:4065103 | pubmed:language | eng | lld:pubmed |
pubmed-article:4065103 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:4065103 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:4065103 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:4065103 | pubmed:month | Aug | lld:pubmed |
pubmed-article:4065103 | pubmed:issn | 0261-4189 | lld:pubmed |
pubmed-article:4065103 | pubmed:author | pubmed-author:KabschWW | lld:pubmed |
pubmed-article:4065103 | pubmed:author | pubmed-author:MannherzH GHG | lld:pubmed |
pubmed-article:4065103 | pubmed:author | pubmed-author:SuckDD | lld:pubmed |
pubmed-article:4065103 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:4065103 | pubmed:volume | 4 | lld:pubmed |
pubmed-article:4065103 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:4065103 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:4065103 | pubmed:pagination | 2113-8 | lld:pubmed |
pubmed-article:4065103 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:4065103 | pubmed:year | 1985 | lld:pubmed |
pubmed-article:4065103 | pubmed:articleTitle | Three-dimensional structure of the complex of actin and DNase I at 4.5 A resolution. | lld:pubmed |
pubmed-article:4065103 | pubmed:publicationType | Journal Article | lld:pubmed |
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