Tej P.

Singh
Tej P. Singh (born 1944) is an Indian biophysicist
known for his work in the elds of Rational
Structure-based drug design, Protein Structure biology and X-ray crystallography. He has played an
active role in the development of drug design in
the elds of Antibacterial therapeutics,[1][2][3][4][5]
Tuberculosis,[6][7][8] Inammation,[9][10] Cancer[11][12]
and Gastropathy.[13][14]

proteins from plant seeds and various serine proteases

and their inhibitors have been determined by his group.
The elaborate structural studies of proteins from several important systems as potential drug targets such
as phospholipase A2, cyclooxygenase, lipoxygenase,
endothelin receptor, endothelin converting enzyme,
breast cancer regression proteins and matrix metanosomal proteins as well as their complexes with natural and
designed synthetic ligands have been carried out. He had
developed the rules of peptide design with alpha, beta
dehydro - amino acids through extensive studies using
syntheses, and X-ray and NMR structure determinations.
These design rules are being exploited for making specic peptides to act as tight inhibitors of target enzymes
and potent antagonists of target receptors for eventually
leading to useful therapeutic agents.

He is a fellow of six academies, namely, the Third World

Academy of Sciences, Indian National Science Academy,
National Academy of Sciences Idian Academy of Sciences, Alexander von Humboldt Foundation and Biotech
Research Society of India.[15]

Education

He initiated a new programme on Clinical Proteomics at

the All India Institute of Medical Sciences in which it is
Tej obtained his Masters in Science from the University
intended to characterize all the proteins that are expressed
of Allahabad. He started his research career in 1971
during various patho/physiological conditions. The newly
as a graduate student at the Indian Institute of Science,
identied proteins will either be useful as biomarkers or
Bangalore. He obtained his Ph. D degree in the mid 70s
they may be associated with the progression of diseases
working on the crystal structure determinations and demaking them important targets for drug design.
sign of anti-inammatory analgesics for new drug discovery.

4 Awards and honors

2

Professional career

Tej is a Fellow of the Third World Academy of Sciences,

Indian National Science Academy, National Academy of
Sciences Indian Academy of Sciences, Alexander von
Humboldt Foundation and Biotech Research Society of
India. He has won the Goyal Prize for Life Sciences,
Distinguished Biotechnology Research Professor (DBT)
(2009), GN Ramachandran Gold Medal for excellence in
Science and Technology (CSIR) (2006) , Distinguished
Biotechnologist (DBT), 2006, JC Bose Memorial Award
(2005), Alexander von Humboldt Fellow (1977), Canadian development Agency Award (1999)

Soon after obtaining his Ph. D degree, Tej worked for

an year as a lecturer at the University of Indore. He then
spent more than two years (19781980) as an Alexander von Humboldt / Max-Planck, post doctoral fellow in
the German laboratory of Professor Robert Huber, who
later received the Nobel Prize. After his return to India
he worked as a reader at Sardar Patel University (1980
83) and an Additional Professor (198485) in the Department of Biophysics at the All India Institute of Medical
Sciences, New Delhi. He was appointed Professor and
Head of the Department in 1986.

5 External links
3

Contributions in Protein Structural Biology

http://dst.gov.in/whats_new/press-release07/
biotech-award.htm
http://www.jbc.org/cgi/reprint/M208967200v1.
pdf

The three-dimensional structures of various proteins

including lactoperoxidase,[16] peptidoglycan recognition
protein, lactoferrin [17][18][19] from several species,
ribosome inactivating proteins,[20] bifunctional inhibitor

http://articles.timesofindia.indiatimes.
com/2004-06-25/delhi/27169560_1_
1

REFERENCES

snake-venom-poisonous-snakes-joint-pain

from a Gram-positive bacterium, Streptococcus pyogenes

at 2.19 resolution shows the closed structure of the
http://www.bio-medicine.org/medicine-news/
substrate-binding cleft. FEBS open bio. 4: 915922.
Five-New-Anti-Inflammatory-Compounds-Produced-By-Indian-Scientists-6838-1/
doi:10.1016/j.fob.2014.10.010. ISSN 2211-5463. PMC
4226762 . PMID 25389518.

References

[1] Sharma, Pradeep; Dube, Divya; Sinha, Mau; Yadav,

Savita; Kaur, Punit; Sharma, Sujata; Singh, Tej P.
(2013-01-01). Structural insights into the dual strategy of recognition by peptidoglycan recognition protein,
PGRP-S: structure of the ternary complex of PGRP-S
with lipopolysaccharide and stearic acid. PloS One. 8
(1): e53756. doi:10.1371/journal.pone.0053756. ISSN
1932-6203. PMC 3541179 . PMID 23326499.
[2] Singh, Amit Kumar; Singh, Nagendra; Sharma, Sujata; Singh, S. Baskar; Kaur, Punit; Bhushan, A.;
Srinivasan, A.; Singh, Tej P. (2008-02-29). Crystal
structure of lactoperoxidase at 2.4 A resolution.
Journal of Molecular Biology.
376 (4): 1060
1075. doi:10.1016/j.jmb.2007.12.012. ISSN 10898638. PMID 18191143.
[3] Rastogi, Nilisha; Nagpal, Nitish; Alam, Hammad;
Pandey, Sadanand; Gautam, Lovely; Sinha, Mau;
Shin, Kouichirou; Manzoor, Nikhat; Virdi, Jugsharan S. (2014-01-01). Preparation and antimicrobial
action of three tryptic digested functional molecules
of bovine lactoferrin. PloS One. 9 (3): e90011.
doi:10.1371/journal.pone.0090011. ISSN 1932-6203.
PMC 3940724 . PMID 24595088.
[4] Rastogi, Nilisha; Singh, Avinash; Pandey, Sada Nand;
Sinha, Mau; Bhushan, Asha; Kaur, Punit; Sharma, Sujata; Singh, Tej P. (2014-06-01). Structure of the
iron-free true C-terminal half of bovine lactoferrin produced by tryptic digestion and its functional signicance
in the gut. The FEBS journal. 281 (12): 2871
2882. doi:10.1111/febs.12827. ISSN 1742-4658. PMID
24798798.
[5] Singh, Avinash; Gautam, Lovely; Sinha, Mau; Bhushan,
Asha; Kaur, Punit; Sharma, Sujata; Singh, T. P. (201401-01). Crystal structure of peptidyl-tRNA hydrolase
from a Gram-positive bacterium, Streptococcus pyogenes
at 2.19 resolution shows the closed structure of the
substrate-binding cleft. FEBS open bio. 4: 915922.
doi:10.1016/j.fob.2014.10.010. ISSN 2211-5463. PMC
4226762 . PMID 25389518.
[6] Sharma, Pradeep; Yamini, Shavait; Dube, Divya; Singh,
Amar; Mal, Gorakh; Pandey, Nisha; Sinha, Mau;
Singh, Abhay Kumar; Dey, Sharmistha (2013-01-01).
Structural basis of the binding of fatty acids to peptidoglycan recognition protein, PGRP-S through second binding site. Archives of Biochemistry and Biophysics. 529
(1): 110. doi:10.1016/j.abb.2012.11.001. ISSN 10960384. PMID 23149273.
[7] Singh, Avinash; Gautam, Lovely; Sinha, Mau; Bhushan,
Asha; Kaur, Punit; Sharma, Sujata; Singh, T. P. (201401-01). Crystal structure of peptidyl-tRNA hydrolase

[8] Singh, Avinash; Kumar, Ashok; Gautam, Lovely; Sharma,

Pradeep; Sinha, Mau; Bhushan, Asha; Kaur, Punit;
Sharma, Sujata; Arora, Ashish (2014-11-01). Structural
and binding studies of peptidyl-tRNA hydrolase from
Pseudomonas aeruginosa provide a platform for the
structure-based inhibitor design against peptidyl-tRNA
hydrolase. The Biochemical Journal. 463 (3): 329
337. doi:10.1042/BJ20140631. ISSN 1470-8728. PMID
25101795.
[9] Shukla, Prakash Kumar; Gautam, Lovely; Sinha,
Mau; Kaur, Punit; Sharma, Sujata; Singh, Tej P.
(2015-04-01). Structures and binding studies of the
complexes of phospholipase A2 with ve inhibitors.
Biochimica et Biophysica Acta. 1854 (4): 269277.
doi:10.1016/j.bbapap.2014.12.017. ISSN 0006-3002.
PMID 25541253.
[10] Sharma, Pradeep; Dube, Divya; Singh, Amar; Mishra,
Biswajit; Singh, Nagendra; Sinha, Mau; Dey, Sharmistha;
Kaur, Punit; Mitra, Dipendra K. (2011-05-06).
Structural basis of recognition of pathogen-associated
molecular patterns and inhibition of proinammatory cytokines by camel peptidoglycan recognition protein. The
Journal of Biological Chemistry. 286 (18): 1620816217.
doi:10.1074/jbc.M111.228163. ISSN 1083-351X. PMC
3091228 . PMID 21454594.
[11] Bilgrami, Sameeta; Yadav, Savita; Kaur, Punit; Sharma,
Sujata; Perbandt, Markus; Betzel, Christian; Singh,
Tej P. (2005-08-23). Crystal structure of the disintegrin heterodimer from saw-scaled viper (Echis carinatus) at 1.9 A resolution. Biochemistry. 44 (33):
1105811066. doi:10.1021/bi050849y. ISSN 00062960. PMID 16101289.
[12] Mohanty, Ashok K.; Singh, Garima; Paramasivam, Murugan; Saravanan, Kolandaivelu; Jabeen, Talat; Sharma,
Sujata; Yadav, Savita; Kaur, Punit; Kumar, Pravindra
(2003-04-18). Crystal structure of a novel regulatory
40-kDa mammary gland protein (MGP-40) secreted during involution. The Journal of Biological Chemistry.
278 (16): 1445114460. doi:10.1074/jbc.M208967200.
ISSN 0021-9258. PMID 12529329.
[13] Sharma, Pradeep; Dube, Divya; Singh, Amar; Mishra,
Biswajit; Singh, Nagendra; Sinha, Mau; Dey, Sharmistha;
Kaur, Punit; Mitra, Dipendra K. (2011-05-06).
Structural basis of recognition of pathogen-associated
molecular patterns and inhibition of proinammatory cytokines by camel peptidoglycan recognition protein. The
Journal of Biological Chemistry. 286 (18): 1620816217.
doi:10.1074/jbc.M111.228163. ISSN 1083-351X. PMC
3091228 . PMID 21454594.
[14] Mir, Raa; Singh, Nagendra; Vikram, Gopalakrishnapillai; Sinha, Mau; Bhushan, Asha; Kaur, Punit; Srinivasan, Alagiri; Sharma, Sujata; Singh, Tej P. (2010-0815). Structural and binding studies of C-terminal half

(C-lobe) of lactoferrin protein with COX-2-specic nonsteroidal anti-inammatory drugs (NSAIDs)". Archives
of Biochemistry and Biophysics.
500 (2): 196
202. doi:10.1016/j.abb.2010.05.026. ISSN 1096-0384.
PMID 20515646.
[15] http://www.brsi.in/#brsi
[16] Singh, A..; Singh, N.; Sharma, S.; Singh, S.B.; Kaur,
P.; Bhushan, A.; Srinivasan, A.; Singh, T.P. (14 December 2007). Crystal structures of lactoperoxidase at
2.4 A resolution. Journal of Molecular Biology. 376
(4): 10601075. doi:10.1016/j.jmb.2007.12.012. PMID
18191143.
[17] Sharma, S.; Jasti, J.; Kumar, J.; Mohanty, A.K.; Singh,
T.P. (8 August 2003). Crystal structure of a proteolytically generated functional monoferric C-lobe of
bovine lactoferrin at 1.9A resolution.. Journal of Molecular Biology. 331 (2): 48596. doi:10.1016/s00222836(03)00717-4. PMID 12888354.
[18] Khan, J.A.; Kumar, P.; Paramasivam, M.; Yadav, R.S.;
Sahani, M.S.; Sharma, S.; Srinivasan, A.; Singh, T.P.
(8 June 2001). Camel lactoferrin, a transferrin-cumlactoferrin: crystal structure of camel apolactoferrin at
2.6 A resolution and structural basis of its dual role..
Journal of Molecular Biology. 309 (3): 751761.
doi:10.1006/jmbi.2001.4692. PMID 11397094.
[19] Mir, R.; Singh, N.; Vikram, G.; Kumar, R.P.; Sinha,
M.; Bhushan, A.; Kaur, P.; Srinivasan, A.; Sharma, S.;
Singh, T.P. (16 December 2009). The structural basis for the prevention of nonsteroidal antiinammatory
drug-induced gastrointestinal tract damage by the C-lobe
of bovine colostrum lactoferrin.. Biophysical Journal.
97 (12): 31783186. doi:10.1016/j.bpj.2009.09.030.
PMID 20006955.
[20] Kushwaha, G.S.; Pandey, N.; Sinha, M.; Singh, S.B.;
Kaur, P.; Sharma, S.; Singh, T.P. (April 2012). Crystal structures of a type-1 ribosome inactivating protein from Momordica balsamina in the bound and unbound states.. Biochimica et Biophysica Acta. 1824
(4): 67991. doi:10.1016/j.bbapap.2012.02.005. PMID
22361570.

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