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Secondary structure and disulfide bonds in CTLDs

Six different disulfide bonds have been described in CTLDs (numbered 1-6 in the diagrams below), although any given CTLD contains only a subset of these linkages.  The presence of single cysteine residues at positions 7, 8 and 9 is usually associated with homo- and hetero-dimer formation. 

The top diagram illustrates all the disulfide bonds which have been described in CTLDs, while the diagrams A to S below illustrate examples of disulfide bond combinations found in CTLD-containing proteins.  The diagrams also depict regions of secondary structure in the CTLD fold: alpha-helices, α 1-2; beta-sheets, β 1-5; and loop regions L 1-4.  These regions of secondary structure can be identified in the structure of a CTLD shown to the left.

A        

B         

C 

D 

E 

F 

G 

H 

I  

J 

K 

L 

M 

N 

O 

P 

Q 

R 

S 

This page last updated:

Thursday, 22 June 2006

Animal lectins home

 

Kurt Drickamer

Division of Molecular Biosciences

Faculty of Natural Sciences

Imperial College London

 

Email: k.drickamer@imperial.ac.uk