Source:http://linkedlifedata.com/resource/pubmed/id/15122922
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
18
|
pubmed:dateCreated |
2004-5-4
|
pubmed:databankReference | |
pubmed:abstractText |
In the frame of a research aimed at the detailed structural characterization of human calcium-binding proteins of the EF-hand family, the solution structure of human alpha-parvalbumin has been solved by NMR and refined with the help of substitution of the Ca(2+) ion in the EF site with the paramagnetic Dy(3+) ion. A simple (1)H-(15)N HSQC spectrum allowed the NH assignments based on the properties of Dy(3+). This allowed us to exploit pseudocontact shifts and residual dipolar couplings for solution structure refinement. The backbone and heavy atom RMSD are 0.55 +/- 0.08 and 1.02 +/- 0.08 A, respectively, and decrease to 0.39 +/- 0.05 and 0.90 +/- 0.06 A upon refinement with paramagnetism-based restraints. The RMSD for the metal itself in the EF site in the refined structure is 0.26 +/- 0.12 A. Backbone NH R(1), R(2), and NOE measured at two temperatures show the protein to be relatively rigid. The NH orientations are well determined by the paramagnetism-based restraints. This allows us to detect small but significant local structural differences with the orthologue protein from rat, whose X-ray structure is available at 2.0 A resolution. All differences are related to local changes in the amino acidic composition.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amides,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon Isotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Dysprosium,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrogen Isotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Parvalbumins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Protons,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0006-2960
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
11
|
pubmed:volume |
43
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
5562-73
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:15122922-Amides,
pubmed-meshheading:15122922-Animals,
pubmed-meshheading:15122922-Anisotropy,
pubmed-meshheading:15122922-Calcium-Binding Proteins,
pubmed-meshheading:15122922-Carbon Isotopes,
pubmed-meshheading:15122922-Crystallography, X-Ray,
pubmed-meshheading:15122922-Dysprosium,
pubmed-meshheading:15122922-EF Hand Motifs,
pubmed-meshheading:15122922-Humans,
pubmed-meshheading:15122922-Models, Molecular,
pubmed-meshheading:15122922-Nitrogen Isotopes,
pubmed-meshheading:15122922-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:15122922-Parvalbumins,
pubmed-meshheading:15122922-Protein Conformation,
pubmed-meshheading:15122922-Protein Isoforms,
pubmed-meshheading:15122922-Protons,
pubmed-meshheading:15122922-Rats,
pubmed-meshheading:15122922-Solutions
|
pubmed:year |
2004
|
pubmed:articleTitle |
Paramagnetism-based refinement strategy for the solution structure of human alpha-parvalbumin.
|
pubmed:affiliation |
Magnetic Resonance Centre and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|