Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5020
|
| pubmed:dateCreated |
1991-9-16
|
| pubmed:abstractText |
The high-resolution three-dimensional structure of a single immunoglobulin binding domain (B1, which comprises 56 residues including the NH2-terminal Met) of protein G from group G Streptococcus has been determined in solution by nuclear magnetic resonance spectroscopy on the basis of 1058 experimental restraints. The average atomic root-mean-square distribution about the mean coordinate positions is 0.27 angstrom (A) for the backbone atoms, 0.65 A for all atoms, and 0.39 A for atoms excluding disordered surface side chains. The structure has no disulfide bridges and is composed of a four-stranded beta sheet, on top of which lies a long helix. The central two strands (beta 1 and beta 4), comprising the NH2- and COOH-termini, are parallel, and the outer two strands (beta 2 and beta 3) are connected by the helix in a +3x crossover. This novel topology (-1, +3x, -1), coupled with an extensive hydrogen-bonding network and a tightly packed and buried hydrophobic core, is probably responsible for the extreme thermal stability of this small domain (reversible melting at 87 degrees C).
|
| pubmed:commentsCorrections | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0036-8075
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
9
|
| pubmed:volume |
253
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
657-61
|
| pubmed:dateRevised |
2007-3-19
|
| pubmed:meshHeading |
pubmed-meshheading:1871600-Amino Acid Sequence,
pubmed-meshheading:1871600-Bacterial Proteins,
pubmed-meshheading:1871600-Binding Sites,
pubmed-meshheading:1871600-Calorimetry,
pubmed-meshheading:1871600-Hydrogen Bonding,
pubmed-meshheading:1871600-Immunoglobulin G,
pubmed-meshheading:1871600-Magnetic Resonance Spectroscopy,
pubmed-meshheading:1871600-Models, Molecular,
pubmed-meshheading:1871600-Protein Conformation
|
| pubmed:year |
1991
|
| pubmed:articleTitle |
A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G.
|
| pubmed:affiliation |
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|