Linked Life Data

11479026

Source:http://linkedlifedata.com/resource/pubmed/id/11479026

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-7-31
pubmed:abstractText
Legume lectins family of proteins, despite having the same 'jelly roll' tertiary structural fold at monomeric level, exhibit considerable variation in their quaternary structure arising out of small changes in their sequence. Nevertheless, their folding behavior and stability correlates very well with their patterns of assembly into dimers and tetramers. A conservation of their fold during evolution, its wide distribution in many protein families together with the availability of structural information on them make them interesting as proteins to explore the effect of inter- versus intra-subunit interactions in the stability of multimeric proteins. Additionally, as 'natural mutants' of quaternary association, proteins of legume lectin family provide interesting paradigms for studies addressing the effect of subunit oligomerization on the stability, folding and function as well as the evolution of multimeric structures.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
1527
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
102-11
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Legume lectin family, the 'natural mutants of the quaternary state', provide insights into the relationship between protein stability and oligomerization.
pubmed:affiliation
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012.
pubmed:publicationType
Journal Article, Comparative Study, Review, Research Support, Non-U.S. Gov't