Crystal Structure of the Peanut Lectin-T-Antigen Complex. Carbohydrate Specificity Generated by Water Bridges

Preparation and preliminary x-ray studies of three acidic pH crystal forms of the anti-T lectin from peanut (Arachis hypogaea)

Salunke, DM
Khan, Islam M
Surolia, A
Vijayan, M

May 1983

Lectins, by definition, are multivalent carbohydrate binding proteins. Their earlier generic name 'p...

A Novel mode of Carbohydrate Recognition in Jacalin, Moraceae Plant Lectin with a Beta-Prism Fold

Sankaranarayanan, Rajan
Sekar, Kanakaraj
Banerjee, Rahul
Vivek, Sharma
Surolia, Avadhesha
Vijayan, Mamannamana

July 1996

Jacalin, a tetrameric two-chain lectin (66,000 M-r) from jackfruit seeds, is highly specific for the...

The crystal structure of a plant lectin in complex with the Tn antigen

Babino, Alvaro
Tello, Diana
Rojas, Adriana
Bay, Sylvie
Osinaga, Eduardo
Alzari, Pedro M

February 2003

AbstractThe structure of the tetrameric Vicia villosa isolectin B4 (VVLB4) in complex with a cancer ...

Crystal Structure of the Peanut Lectin-T-Antigen Complex. Carbohydrate Specificity Generated by Water Bridges

Ravishankar, R
Ravindran, M
Suguna, K
Surolia, A
Vijayan, M

June 1997

Peanut lectin binds with high specificity to the tumour associated disaccharide Galbeta-1-3GalNAc, g...

Crystal structure of the peanut lectin - T-antigen complex. Carbohydrate specificity generated by water bridges

Ravishankar, R.
Ravindran, M.
Suguna, K.
Surolia, A.
Vijayan, M.

June 1997

Peanut lectin binds with high specificity to the tumour associated disaccharide GaI.81-3GaINAc, gen...

Structural studies on peanut lectin complexed with disaccharides involving different linkages: further insights into the structure and interactions of the lectin

Natchiar, S. K.
Srinivas, O.
Mitra, N.
Surolia, A.
Jayaraman, N.
Vijayan, M.

November 2006

Crystal structures of peanut lectin complexed with Galβ1-3Gal, methyl-T-antigen, Galβ1-6GalNAc, Galα...

Structures of the complexes of peanut lectin with methyl-β-galactose and N-acetyllactosamine and a comparative study of carbohydrate binding in Gal/GalNAc-specific legume lectins

Ravishankar, R.
Suguna, K.
Surolia, A.
Vijayan, M.

August 1999

The crystal structures of complexes of peanut lectin with methyl-β-galactose and N-acetyllactosamine...

Structures of the complexes of peanut lectin with methyl-$\beta$-galactose and N-acetyllactosamine and a comparative study of carbohydrate binding in Gal/GalNAc-specific legume lectins

Ravishankar, R
Suguna, K
Surolia, A
Vijayan, M

August 1999

The crystal structures of complexes of peanut lectin with methyl-galactose and N-acetyllactosamine h...

Crystal Structure of the Jacalin–T-antigen Complex and a Comparative Study of Lectin–T-antigen Complexes

Jeyaprakash, Arockia A
Rani, Geetha P
Reddy, Banuprakash G
Banumathi, S
Betzel, C
Sekar, K
Surolia, A
Vijayan, M

August 2002

Thomsen–Friedenreich antigen (Galbeta1–3GalNAc), generally known as T-antigen, is expressed in more ...

Crystal structure of the jacalin-T-antigen complex and a comparative study of lectin-T-antigen complexes

A. Arockia Jeyaprakash
P. Geetha Rani
G. Banuprakash Reddy
S. Banumathi
C. Betzel
K. Sekar
A. Surolia
M. Vijayan
Fur Medizinische Biochemie

January 2002

Thomsen–Friedenreich antigen (Galb1–3GalNAc), generally known as T-antigen, is expressed in more tha...

Peanut agglutinin, a lectin with an unusual quaternary structure and interesting ligand binding properties

Kundhavai Natchiar, S.
Suguna, K.
Surolia, A.
Vijayan, M.

January 2007

Lectins are multivalent proteins which play their biological role through the ability to specificall...

Mutational Analysis at Asn-41 in Peanut Agglutinin - A Residue Critical For The Binding Of The Tumor-Associated Thomsen-Friedenreich Antigen

Adhikari, Pratima
Sikder, Bachhawat K
Thomas, Celestine J
Ravishankar, R
Jeyaprakash, Arockia A
Sharma, Vivek
Vijayan, Mamanamana
Surolia, Avadhesha

November 2001

Peanut agglutinin is a clinically important lectin due to its application in the screening of mature...

Mutational analysis at Asn-41 in peanut agglutinin - a residue critical for the binding of the tumor-associated Thomsen-Friedenreich antigen

Adhikari, Pratima
Bachhawat-Sikder, Kiran
Thomas, Celestine J.
Ravishankar, R.
Arockia Jeyaprakash, A.
Sharma, Vivek
Vijayan, Mamanamana
Surolia, Avadhesha

November 2001

Peanut agglutinin is a clinically important lectin due to its application in the screening of mature...

Crystal structure of peanut lectin, a protein with an unusual quaternary structure

Banerjee, R
Mande, SC
Ganesh, V
Das, K
Dhanaraj, V
Mahanta, SK
Suguna, K
Surolia, Avadhesha
Vijayan, M

January 1994

The x-ray crystal structure of the tetrameric T-antigen-binding lectin from peanut, M(r) 110,000, ha...

Imparting Exquisite Specificity to Peanut Agglutinin for the Tumor-associated Thomsen-Friedenreich Antigen by Redesign of Its Combining Site

Sharma, Vivek
Vijayan, M
Surolia, Avadhesha

August 1996

Lectins from legumes constitute one of the most thoroughly studied families of proteins, yet the abs...

Preparation and preliminary x-ray studies of three acidic pH crystal forms of the anti-T lectin from peanut (Arachis hypogaea)

Salunke, DM
Khan, Islam M
Surolia, A
Vijayan, M

May 1983

Lectins, by definition, are multivalent carbohydrate binding proteins. Their earlier generic name 'p...

A Novel mode of Carbohydrate Recognition in Jacalin, Moraceae Plant Lectin with a Beta-Prism Fold

Sankaranarayanan, Rajan
Sekar, Kanakaraj
Banerjee, Rahul
Vivek, Sharma
Surolia, Avadhesha
Vijayan, Mamannamana

July 1996

Jacalin, a tetrameric two-chain lectin (66,000 M-r) from jackfruit seeds, is highly specific for the...

The crystal structure of a plant lectin in complex with the Tn antigen

Babino, Alvaro
Tello, Diana
Rojas, Adriana
Bay, Sylvie
Osinaga, Eduardo
Alzari, Pedro M

February 2003

AbstractThe structure of the tetrameric Vicia villosa isolectin B4 (VVLB4) in complex with a cancer ...

Crystal Structure of the Peanut Lectin-T-Antigen Complex. Carbohydrate Specificity Generated by Water Bridges

Ravishankar, R
Ravindran, M
Suguna, K
Surolia, A
Vijayan, M

June 1997

Peanut lectin binds with high specificity to the tumour associated disaccharide Galbeta-1-3GalNAc, g...

Crystal structure of the peanut lectin - T-antigen complex. Carbohydrate specificity generated by water bridges

Ravishankar, R.
Ravindran, M.
Suguna, K.
Surolia, A.
Vijayan, M.

June 1997

Peanut lectin binds with high specificity to the tumour associated disaccharide GaI.81-3GaINAc, gen...

Structural studies on peanut lectin complexed with disaccharides involving different linkages: further insights into the structure and interactions of the lectin

Natchiar, S. K.
Srinivas, O.
Mitra, N.
Surolia, A.
Jayaraman, N.
Vijayan, M.

November 2006

Crystal structures of peanut lectin complexed with Galβ1-3Gal, methyl-T-antigen, Galβ1-6GalNAc, Galα...

Structures of the complexes of peanut lectin with methyl-β-galactose and N-acetyllactosamine and a comparative study of carbohydrate binding in Gal/GalNAc-specific legume lectins

Ravishankar, R.
Suguna, K.
Surolia, A.
Vijayan, M.

August 1999

The crystal structures of complexes of peanut lectin with methyl-β-galactose and N-acetyllactosamine...

Structures of the complexes of peanut lectin with methyl-$\beta$-galactose and N-acetyllactosamine and a comparative study of carbohydrate binding in Gal/GalNAc-specific legume lectins

Ravishankar, R
Suguna, K
Surolia, A
Vijayan, M

August 1999

The crystal structures of complexes of peanut lectin with methyl-galactose and N-acetyllactosamine h...

Crystal Structure of the Jacalin–T-antigen Complex and a Comparative Study of Lectin–T-antigen Complexes

Jeyaprakash, Arockia A
Rani, Geetha P
Reddy, Banuprakash G
Banumathi, S
Betzel, C
Sekar, K
Surolia, A
Vijayan, M

August 2002

Thomsen–Friedenreich antigen (Galbeta1–3GalNAc), generally known as T-antigen, is expressed in more ...

Crystal structure of the jacalin-T-antigen complex and a comparative study of lectin-T-antigen complexes

A. Arockia Jeyaprakash
P. Geetha Rani
G. Banuprakash Reddy
S. Banumathi
C. Betzel
K. Sekar
A. Surolia
M. Vijayan
Fur Medizinische Biochemie

January 2002

Thomsen–Friedenreich antigen (Galb1–3GalNAc), generally known as T-antigen, is expressed in more tha...

Peanut agglutinin, a lectin with an unusual quaternary structure and interesting ligand binding properties

Kundhavai Natchiar, S.
Suguna, K.
Surolia, A.
Vijayan, M.

January 2007

Lectins are multivalent proteins which play their biological role through the ability to specificall...

Mutational Analysis at Asn-41 in Peanut Agglutinin - A Residue Critical For The Binding Of The Tumor-Associated Thomsen-Friedenreich Antigen

Adhikari, Pratima
Sikder, Bachhawat K
Thomas, Celestine J
Ravishankar, R
Jeyaprakash, Arockia A
Sharma, Vivek
Vijayan, Mamanamana
Surolia, Avadhesha

November 2001

Peanut agglutinin is a clinically important lectin due to its application in the screening of mature...

Mutational analysis at Asn-41 in peanut agglutinin - a residue critical for the binding of the tumor-associated Thomsen-Friedenreich antigen

Adhikari, Pratima
Bachhawat-Sikder, Kiran
Thomas, Celestine J.
Ravishankar, R.
Arockia Jeyaprakash, A.
Sharma, Vivek
Vijayan, Mamanamana
Surolia, Avadhesha

November 2001

Peanut agglutinin is a clinically important lectin due to its application in the screening of mature...

Crystal structure of peanut lectin, a protein with an unusual quaternary structure

Banerjee, R
Mande, SC
Ganesh, V
Das, K
Dhanaraj, V
Mahanta, SK
Suguna, K
Surolia, Avadhesha
Vijayan, M

January 1994

The x-ray crystal structure of the tetrameric T-antigen-binding lectin from peanut, M(r) 110,000, ha...

Imparting Exquisite Specificity to Peanut Agglutinin for the Tumor-associated Thomsen-Friedenreich Antigen by Redesign of Its Combining Site

Sharma, Vivek
Vijayan, M
Surolia, Avadhesha

August 1996

Lectins from legumes constitute one of the most thoroughly studied families of proteins, yet the abs...

Preparation and preliminary x-ray studies of three acidic pH crystal forms of the anti-T lectin from peanut (Arachis hypogaea)

Salunke, DM
Khan, Islam M
Surolia, A
Vijayan, M

May 1983

Lectins, by definition, are multivalent carbohydrate binding proteins. Their earlier generic name 'p...

A Novel mode of Carbohydrate Recognition in Jacalin, Moraceae Plant Lectin with a Beta-Prism Fold

Sankaranarayanan, Rajan
Sekar, Kanakaraj
Banerjee, Rahul
Vivek, Sharma
Surolia, Avadhesha
Vijayan, Mamannamana

July 1996

Jacalin, a tetrameric two-chain lectin (66,000 M-r) from jackfruit seeds, is highly specific for the...

The crystal structure of a plant lectin in complex with the Tn antigen

Babino, Alvaro
Tello, Diana
Rojas, Adriana
Bay, Sylvie
Osinaga, Eduardo
Alzari, Pedro M

February 2003

AbstractThe structure of the tetrameric Vicia villosa isolectin B4 (VVLB4) in complex with a cancer ...

Crystal Structure of the Peanut Lectin-T-Antigen Complex. Carbohydrate Specificity Generated by Water Bridges

Abstract

Extracted data

Crystal Structure of the Peanut Lectin-T-Antigen Complex. Carbohydrate Specificity Generated by Water Bridges

Abstract

Extracted data

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