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PDBsum entry 1qg3
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Structural protein
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PDB id
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1qg3
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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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Crystal structure of a tandem pair of fibronectin type III domains from the cytoplasmic tail of integrin alpha6beta4.
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Authors
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J.M.De pereda,
G.Wiche,
R.C.Liddington.
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Ref.
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EMBO J, 1999,
18,
4087-4095.
[DOI no: ]
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PubMed id
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Abstract
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The integrin alpha6beta4 is an essential component of hemidesmosomes but it also
plays a dynamic role in invasive carcinoma cells. The cytoplasmic tail of the
beta4 subunit is uniquely large among integrins and includes two pairs of
fibronectin type III domains separated by a connecting segment. Here we describe
the crystal structure of the first tandem domain pair, a module that is critical
for alpha6beta4 function. The structure reveals a novel interdomain interface
and candidate protein-binding sites, including a large acidic cleft formed from
the surfaces of both domains and a prominent loop that is reminiscent of the RGD
integrin-binding loop of fibronectin. This is the first crystal structure of
either a hemidesmosome component or an integrin cytoplasmic domain, and it will
enable the intracellular functions of alpha6beta4 to be dissected at the atomic
level.
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Figure 3.
Figure 3 Stereo close-up of the interdomain interface. Selected
residues are shown in ball-and-stick form; hydrogen bonds
between linker side chains and domain loops are indicated by
dashed lines. The view is rotated by 180° about a vertical
axis compared with Figure 1B.
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Figure 5.
Figure 5 Electron density maps of the C–C' loop of domain 2.
The refined structure of the loop is shown in ball-and-stick
form. (A) Experimental solvent flattened map at 2.8 Å
resolution, contoured at 1  .
(B) 2F[o]-F[c] map with phases calculated from the final model
at 2.15 Å, contoured at 1 .
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(1999,
18,
4087-4095)
copyright 1999.
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