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 COLLAGEN

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COLLAGEN
 COLLAGEN
ollagens illustrates diverse
structure--function relationships
structure

Ô Collagen of tendons ± forms highly asymmetric structures of high

tensile strength
Ô Skin collagen ± forms loosely woven, flexible fibers
Ô Collagen of hard regions of teeth & bone ± contains
hydroxyapatite, a calcium phosphate polymer
Ô Collagen in the cornea ± nearly crystalline, transparent
 COLLAGEN
ºropocollagen is a ºriple Helical molecule
Rich in Gly, Pro, and Hyp



uu consist of 3 approximately 1000uresidue

º



polypeptide chains organized as leftuhanded nonu uhelix
that has approximately three residues per turn.
Three leftuhanded helices entwine to form a rightuhanded
triple helix, or supercoil stabilized by hydrogen bonds
formed between individual polypeptide chains.
 COLLAGEN
º




The supercoil resists unwinding because it and its

three polypeptides are coiled in opposite directions.

The highly asymmetric mature collagen fibers

measures 1.5 nm by about 300 nm, reflecting their
stable, extended conformation.

  




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chains coiled about each other into a rightuhanded triple helixes
 COLLAGEN
pvery third residue is Glycine

(Gly-X-Pro/Hyp)n

The primary structural motif of mature collagen.

Every 3rd residue is Glycine, the only residue with an R group
small enough to fit within the central core of the superhelix.
Each Glycine is preceded by either a Prolyl or Hydroxyprolyl
residue.
 COLLAGEN
ëany Posttranslational modifications
haracterize Procollagen maturation

Procollagen
collagen precursor with the carboxyl and amino terminals have an amino acid
composition typical of a globular protein.
During maturation of procollagen, these carboxyl and amino terminal extensions
are removed by selective proteolysis.
Hydroxylation of prolyl and lysyl residues is catalyzed by prolyl hydroxylase
and lysyl hyroxylase ± enzymes that require ascorbic acid (vit. C)
Specific hydroxylysyl residues are then glycosylated by galactosyl and glucosyl
transferases.
 COLLAGEN
ovalent cross-
cross-links stabilize collagen fibers
Tropocollagen associate to form collagen microfibrils.

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Ô intrachain hydrogen bonds
Ô Covalent bonds formed within & between helices

*This covalent crossulinking process involves the copperurequiring enzyme




 which converts the nonu uamino groups of hydroxyl residues to
aldehydes.
*These aldehydes then either undergo an aldol condensation or condense with
the nonu uamino groups of lysine or hydroxylysine, forming £



 COLLAGEN
autritional an Genetic disorders
an involve impaired secondary structure

The medical importance of stable secondary structures

is thoroughly documented by disorders of
tropocollagen biosynthesis and maturation.
 COLLAGEN
Ô £  
 


uprolyl & lysyl hydroxylases are inactive and tropocollagen cannot
undergo the reactions that form covalent crossulinks which results to scurvy

£u nutritional disorder characterized by bleeding gums, poor wound

healing, an ultimately death.

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is caused by a defective gene that regulates the metabolism of copper in the
body. Because it is an Xulinked gene, the disease primarily affects male
infants. Copper accumulates at abnormally low levels in the liver and brain,
but at higher than normal levels in the kidney and intestinal lining. Affected
infants may be born prematurely, characterized by kinky hair and growth
retardation¶
 COLLAGEN

Genetic disorders of collagen biosynthesis include several form

of
 

   characterized by fragile bones.

 


 characterized by mobile joints and
skin abnormalities, reflect defects in the genes that uencode 1u
procollagen, procollagen aupeptidase, or lysyly hydroxylase.
 Vtƍs FRpp to join.
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