Linked Life Data

11513005

Source:http://linkedlifedata.com/resource/pubmed/id/11513005

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 2
pubmed:dateCreated
2001-8-21
pubmed:abstractText
Boar Spermatidal Transition Protein 2 (TP2; 137 amino acid residues) is supposed to play an important role in initiation of chromatin condensation and cessation of transcriptional activity during mammalian spermniogenesis. Boar TP2 has three potential zinc finger motifs and binds three atoms of zinc per molecule. However the structure of the zinc-binding domain of boar TP2 has not been completely determined. To elucidate the local structure around the zinc atoms of boar TP2, we performed an X-ray absorption fine structure (XAFS) measurement on the zinc-binding domain of TP2(TP2Z)(residues 1-103) in the fluorescence mode. By EXAFS analyses we have demonstrated that each of the three zinc atoms is coordinated by approximately two sulfur and two nitrogen atoms on average. The average Zn-S and Zn-N distances were found to be 2.36 and 2.01 A, respectively. The sulfur and nitrogen atoms are attributed to cysteine and histidine residues, respectively, from comparison of the EXAFS spectra with model compounds ZnS and ZnTPP zinc(II) tetraphenylporphyrin).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0909-0495
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
993-5
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
EXAFS analysis of the zinc-binding domain of boar spermatidal transition protein 2.
pubmed:affiliation
Graduate School for Science, Chiba University, Inage, Japan. tkawai@scichem.s.chem.chiba-u.ac.jp
pubmed:publicationType
Journal Article