Legume lectin family, the 'natural mutants of the quaternary state', provide insights into the relationship between protein stability and oligomerization.
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.
Srinivas
V R
VR
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012.
Reddy
G B
GB
Ahmad
N
N
Swaminathan
C P
CP
Mitra
N
N
Surolia
A
A
D000595:Amino Acid Sequence; D002152:Calorimetry, Differential Scanning; D019281:Dimerization; D007887:Fabaceae / Q000737:chemistry*; D037102:Lectins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D037121:Plant Lectins; D010946:Plants, Medicinal; D011489:Protein Denaturation; D017510:Protein Folding; D016415:Sequence Alignment
D037102:Lectins; D037121:Plant Lectins