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PDBsum entry 1e8b
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Cell adhesion
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PDB id
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1e8b
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The hairpin structure of the (6)f1(1)f2(2)f2 fragment from human fibronectin enhances gelatin binding.
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Authors
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A.R.Pickford,
S.P.Smith,
D.Staunton,
J.Boyd,
I.D.Campbell.
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Ref.
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EMBO J, 2001,
20,
1519-1529.
[DOI no: ]
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PubMed id
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Abstract
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The solution structure of the (6)F1(1)F2(2)F2 fragment from the gelatin-binding
region of fibronectin has been determined (Protein Data Bank entry codes 1e88
and 1e8b). The structure reveals an extensive hydrophobic interface between the
non-contiguous (6)F1 and (2)F2 modules. The buried surface area between (6)F1
and (2)F2 ( approximately 870 A(2)) is the largest intermodule interface seen in
fibronectin to date. The dissection of (6)F1(1)F2(2)F2 into the (6)F1(1)F2 pair
and (2)F2 results in near-complete loss of gelatin-binding activity. The hairpin
topology of (6)F1(1)F2(2)F2 may facilitate intramolecular contact between the
matrix assembly regions flanking the gelatin-binding domain. This is the first
high-resolution study to reveal a compact, globular arrangement of modules in
fibronectin. This arrangement is not consistent with the view that fibronectin
is simply a linear 'string of beads'.
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Figure 5.
Figure 5 Module reorganization upon dissection of 6F1^1F2^2F2.
Ribbon diagrams of the minimized average structures of (A)
6F1^1F2^2F2 and (B) 6F1^1F2. The colour scheme for the secondary
structure elements is as in Figure 3A -C. Side chains for which
6F1 -2F2 intermodule NOEs were observed (V10, Y12, S13, M16, L19
and L28 of 6F1, and L103, Q105, S111, N112, A114, L115, T145 and
K153 for 2F2) are shown in cyan for 6F1 and purple for 2F2.
Removal of the 2F2 module allows the side chain of Y68 (pink) in
1F2 to interact with L19 and L28 in 6F1.
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Figure 6.
Figure 6 Global topologies of multimodule fibronectin fragments.
Solvent-accessible surfaces have been superimposed over ribbon
diagrams for the minimized average structure of 6F1^1F2^2F2, and
the crystal structures of 7F3^8F3^9F3^10F3 (Leahy et al., 1996)
and 12F3^13F3^14F3 (Sharma et al., 1999). The fragment
structures are mapped onto the mosaic illustration of
fibronectin, which has been folded to account for the hairpin
structure of 6F1^1F2^2F2.
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2001,
20,
1519-1529)
copyright 2001.
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