Transferrin is a 76 kDa glycoprotein encoded by the TF gene located on chromosome 3 that transports iron in the bloodstream. It is produced primarily in the liver and contains two binding sites for Fe3+ ions. The protein consists of two lobes, the N-lobe and C-lobe, each containing two subdomains made up of alpha helices and beta sheets. Four conserved amino acids play an important role in iron binding and release: two tyrosines, one aspartic acid, and one histidine. Transferrin transports iron throughout the body, and is important for processes like the immune response and cell growth and differentiation.

1. 1
Topic- Transferrin
Session - 2020
Presented By: Chanderhash
"Structure and its effect on function of proteins’’
Course code: BSBT-411

2. Encoded
Human
transferrin is
encoded by
the TF gene and
produced as a
76 kDa
glycoprotein.
Binding
Bind to and
consequently
mediate the
transport
of Iron (Fe)
through blood
plasma.
Amino acid
It consists single
polypeptide chain
of 680 to 700
amino acids.
Location
Produced in liver
and it contain two
binding site
for Fe3+ atoms
Chromosome
no. 3
(3q22.1)
structure
2
Transf
-errin

3. GENE LOCATION
(HUMAN)
3
Chromosome no. 3
Band ---(3q22.1)

4. TF molecules divided into two
lobes:-
a) N-lobe (336 amino acid)
b) C-lobe (343 amino acid)
Each lobe contains two domain comparising a
series of Alpha helices which overlay a central
Beta sheet backbone
4
Structure
Fig."Transcriptional regulation of transferrin and albumin genes by retinoic acid in human hepatoma

5. A s p 2 4 0 a t t h e e n d o f - h e l i x 8 b i n t h e
N 2 - s u b d o m a i n i n t e r a c t s w i t h A r g 6 7 8
a d j a c e n t t o t h e C - t e r m i n a l h e l i x ( h e l i x
1 2 ) i n t h e C 1 - s u b d o m a i n , a n d A r g 3 0 8 i n
t h e N 1 - s u b d o m a i n ( i n t h e l o o p p r i o r t o
h e l i x 1 0 ) i n t e r a c t s w i t h A s p 3 7 6 i n h e l i x
2 o f t h e C 1 - s u b d o m a i n .
It consists at the N and C terminal lobes has four
conserved amino acids
Two Tyrosine
One Aspartic
And One Histadine
5
(N-terminal lobe – Asp-63, Tyr-95, Tyr-188 and His-249Fig."Transcriptional regulation of transferrin and albumin genes by retinoic acid in human hepatoma

6. 6
Structure and sequence of transferrin
http://www.rcsb.org/pdb/
(a)
X-ray crystal structure of
Transferrin
(b)
Amino acid sequence of the
N-terminal lobe of transferrin

7. Immune system
•
innate immune
•
mucosa and bind with
iron.
•
inflammation
Disease
•
iron deficiency
anemia,
Nano-medicine
•
• Alzheimer's
Parkinson's
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9. Targeted drug
delivery
Delivery of
therapeutic
metals, proteins,
drugs and genes
via transferrin–
transferrin
receptor pathway
Cancer therapy
Promote
cytotoxicity and
proliferation of
lymphokine-
activated killer
and natural killer
cells
Bone marrow
transplantation
Antimicrobial
9
Tumor
or
cancer
Growth
and
differentiation
Free
iron

10. Reference
Hirose, M. (2000) The structural mechanism for iron uptake and release by transferrins. Biosci.
Biotechnol. Biochem. 64, 1328–1336
https://biologydictionary.net/transferrin/
He, Q.Y. et al. (2000) The chloride effect is related to anion binding in determining the rate of iron
release from the human transferrin N-lobe. Biochem. J. 350, 909–915
s
http://www.bmj.com/permissions
http://www.rcsb.org/pdb/
Dewan JC, Mikami B, Hirose M, Sacchettini JC (November 1993). "Structural evidence for a pH-
sensitive dilysine trigger in the hen ovotransferrin N-lobe: implications for transferrin iron
release". Biochemistry. 32 (45): 11963–8. doi:10.1021/bi00096a004. PMID 8218271.

11. THANK
YOU
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