Linked Life Data

2568280

Source:http://linkedlifedata.com/resource/pubmed/id/2568280

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1989-8-21
pubmed:abstractText
1. The roles of conserved polar residues have been studied in 12 V-domains for which atomic coordinates are available. 2. In most cases a particular residue had a similar side chain conformation in all V-domains examined and the polar group provided the same hydrogen bonds which helped to stabilize the conformations of the domains. 3. In the case of a conserved glutamine/glutamic acid residue the buried side chain could adopt a variety of conformations and the polar group could form different hydrogen bonds from one domain to another. However, they contributed similarly to domain stability. 4. In the case of a conserved threonine/serine residue its side chain showed relative rotations of up to 180 degrees from one domain to another. The hydroxyl group could be buried or exposed at the domain surface. In some domains it formed hydrogen bonds to two other protein atoms but in other domains there was a single hydrogen bond or none at all. The varied roles of this residue are discussed in the text.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0020-711X
pubmed:author
pubmed:issnType
Print
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
227-32
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Some observations on conserved polar side chains in immunoglobulin V-domains.
pubmed:affiliation
Agricultural and Food Research Council, Institute of Animal Physiology and Genetics Research, Babraham, Cambridge, England.
pubmed:publicationType
Journal Article