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PDBsum entry 1m3d
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Structural protein
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PDB id
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1m3d
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Contents |
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(+ 2 more)
223 a.a.
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222 a.a.
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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 nc1 domains. Structural basis for type IV collagen assembly in basement membranes.
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Authors
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M.Sundaramoorthy,
M.Meiyappan,
P.Todd,
B.G.Hudson.
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Ref.
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J Biol Chem, 2002,
277,
31142-31153.
[DOI no: ]
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PubMed id
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Abstract
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Type IV collagen, which is present in all metazoan, exists as a family of six
homologous alpha(IV) chains, alpha1-alpha6, in mammals. The six chains assemble
into three different triple helical protomers and self-associate as three
distinct networks. The network underlies all epithelia as a component of
basement membranes, which play important roles in cell adhesion, growth,
differentiation, tissue repair and molecular ultrafiltration. The specificity of
both protomer and network assembly is governed by amino acid sequences of the
C-terminal noncollagenous (NC1) domain of each chain. In this study, the
structural basis for protomer and network assembly was investigated by
determining the crystal structure of the ubiquitous [(alpha1)(2).alpha2](2) NC1
hexamer of bovine lens capsule basement membrane at 2.0 A resolution. The NC1
monomer folds into a novel tertiary structure. The (alpha1)(2).alpha2 trimer is
organized through the unique three-dimensional domain swapping interactions. The
differences in the primary sequences of the hypervariable region manifest in
different secondary structures, which determine the chain specificity at the
monomer-monomer interfaces. The trimer-trimer interface is stabilized by the
extensive hydrophobic and hydrophilic interactions without a need for disulfide
cross-linking.
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Figure 3.
Fig. 3. Stereo view of a section of 2Fo  F[c] map
(contoured at 1  ), where
differences between the human and bovine sequences occur (  2: D96E and
E97D) (refer also to Fig. 2 legend).
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Figure 8.
Fig. 8. Comparison of the essential hydrogen bonding
interactions in the interface at the "core" (A) and the "outer"
(B) and major-minor junctions (C) for 1- 1 and 1- 2 dimers at
the trimer-trimer interface (see text for details).
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2002,
277,
31142-31153)
copyright 2002.
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