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1.
Glycobiology ; 16(10): 938-46, 2006 Oct.
Article in English | MEDLINE | ID: mdl-16782824

ABSTRACT

Lectins, a class of carbohydrate-binding proteins, are now widely recognized to play a range of crucial roles in many cell-cell recognition events triggering several important cellular processes. They encompass different members that are diverse in their sequences, structures, binding site architectures, quaternary structures, carbohydrate affinities, and specificities as well as their larger biological roles and potential applications. It is not surprising, therefore, that the vast amount of experimental data on lectins available in the literature is so diverse, that it becomes difficult and time consuming, if not impossible to comprehend the advances in various areas and obtain the maximum benefit. To achieve an effective use of all the data toward understanding the function and their possible applications, an organization of these seemingly independent data into a common framework is essential. An integrated knowledge base ( Lectindb, http://nscdb.bic.physics.iisc.ernet.in ) together with appropriate analytical tools has therefore been developed initially for plant lectins by collating and integrating diverse data. The database has been implemented using MySQL on a Linux platform and web-enabled using PERL-CGI and Java tools. Data for each lectin pertain to taxonomic, biochemical, domain architecture, molecular sequence, and structural details as well as carbohydrate and hence blood group specificities. Extensive links have also been provided for relevant bioinformatics resources and analytical tools. Availability of diverse data integrated into a common framework is expected to be of high value not only for basic studies in lectin biology but also for basic studies in pursuing several applications in biotechnology, immunology, and clinical practice, using these molecules.


Subject(s)
Databases, Protein , Plant Lectins/classification , Algorithms , Amino Acid Sequence , Molecular Sequence Data , Phylogeny , Sequence Homology, Amino Acid
2.
Bioinformatics ; 19(1): 167-8, 2003 Jan.
Article in English | MEDLINE | ID: mdl-12499314

ABSTRACT

SUMMARY: We have developed a WWW server, HBPRINT, for the identification of hydrogen-bond signature patterns in protein families from their structures. The server calculates (a) common hydrogen bonds between two structures (b) a hydrogen-bond fingerprint in a set of structural neighbours and (c) details of conserved hydrogen bonds. The server also enables the visualization of the hydrogen bond network comprising the signature pattern. AVAILABILITY: HBPRINT and a tutorial are available from http://144.16.93.115/hb_page/index.html.


Subject(s)
Conserved Sequence/genetics , Proteins/chemistry , Sequence Alignment/methods , User-Computer Interface , Algorithms , Garlic/chemistry , Hydrogen Bonding , Internet , Plant Lectins/chemistry , Plant Lectins/genetics , Protein Conformation , Proteins/classification , Proteins/genetics , Sequence Analysis, Protein/methods
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