DC Field | Value | Language |
---|---|---|
dc.contributor.author | Jang, SB | ko |
dc.contributor.author | Cho, YS | ko |
dc.contributor.author | Eom, SJ | ko |
dc.contributor.author | Choi, EJ | ko |
dc.contributor.author | Kim, KH | ko |
dc.contributor.author | Suh, PG | ko |
dc.contributor.author | Oh, Byung-Ha | ko |
dc.date.accessioned | 2013-03-06T03:34:09Z | - |
dc.date.available | 2013-03-06T03:34:09Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2002-03 | - |
dc.identifier.citation | ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, v.58, pp.564 - 566 | - |
dc.identifier.issn | 0907-4449 | - |
dc.identifier.uri | http://hdl.handle.net/10203/85699 | - |
dc.description.abstract | SEDL (known also as sedlin) is a 140 amino-acid protein with a putative role in endoplasmic reticulum-to-Golgi transport. Several missense mutations and deletion mutations in the SEDL gene, which result in protein truncation by frame shift, are responsible for spondyloepiphyseal dysplasia tarda, a progressive skeletal disorder. The protein is identical to MIP-2A, which was shown to interact physically with c-myc promotor-binding protein 1 (MBP-1) and relieve the regulatory role of MBP-1 as a general transcription repressor. In order to gain insights into the function of SEDL by structural analysis, the protein was overexpressed and crystallized as a first step. SEDL was overexpressed in Escherichia coli and crystallized using the hanging-drop vapour-diffusion method at 298 K. The crystals belong to the orthorhombic space group C222(1), with unit-cell parameters a = 46.69, b = 101.30, c = 66.15 Angstrom. The unit cell is likely to contain one molecule of SEDL, with a crystal volume per protein mass (V-M) of 2.36 Angstrom(3) Da(-1) and a solvent content of about 47.9% by volume. A native data set to 2.8 Angstrom resolution was obtained from a flash-cooled crystal using synchrotron radiation. | - |
dc.language | English | - |
dc.publisher | BLACKWELL MUNKSGAARD | - |
dc.subject | LINKED SPONDYLOEPIPHYSEAL DYSPLASIA | - |
dc.subject | TARDA | - |
dc.subject | GENE | - |
dc.title | Crystallization and preliminary X-ray crystallographic analysis of SEDL | - |
dc.type | Article | - |
dc.identifier.wosid | 000174227200036 | - |
dc.identifier.scopusid | 2-s2.0-0036514146 | - |
dc.type.rims | ART | - |
dc.citation.volume | 58 | - |
dc.citation.beginningpage | 564 | - |
dc.citation.endingpage | 566 | - |
dc.citation.publicationname | ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | - |
dc.identifier.doi | 10.1107/S0907444902001403 | - |
dc.contributor.localauthor | Oh, Byung-Ha | - |
dc.contributor.nonIdAuthor | Jang, SB | - |
dc.contributor.nonIdAuthor | Cho, YS | - |
dc.contributor.nonIdAuthor | Eom, SJ | - |
dc.contributor.nonIdAuthor | Choi, EJ | - |
dc.contributor.nonIdAuthor | Kim, KH | - |
dc.contributor.nonIdAuthor | Suh, PG | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | LINKED SPONDYLOEPIPHYSEAL DYSPLASIA | - |
dc.subject.keywordPlus | TARDA | - |
dc.subject.keywordPlus | GENE | - |
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