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Figure 4.
FIG. 4. A, superposition of the I-EGF1 domain (red, Protein
Data Bank code 1YUK [PDB]
, this work) with the I-EGF4 from integrin  [3] (blue, Protein Data
Bank code 1JV2 [PDB]
) and the EGF domain of P-selectin (turquoise, Protein Data Bank
code 1FSB [PDB]
). The disulfide bonds C3-C6 and C7-C8 are well conserved,
constraining the fold of the C-terminal part of the EGF module.
The cysteine bridge (C2-C4) is absent in the I-EGF1 domain.
Large conformational variations are observed between the
N-terminal ends of the three structures. The present I-EGF1
structure lacks strand 4 leaving its strand
3
unpaired (see text). B, schematic representation of the I-EGF1
structure of human integrin [2]. The three disulfide
bonds C1-C5, C3-C6, and C7-C8 are indicated. It should be noted
that the cysteines are numbered according to the typical
integrin-EGF domain with 8 cysteines; in this case, C2 and C4
are missing. The Arg and Leu residues that replace C2 and C4,
respectively, according to the published sequence alignment (17)
are in a yellow background.
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