1m3d
From Proteopedia
(New page: 200px<br /><applet load="1m3d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m3d, resolution 2.0Å" /> '''Structure of Type IV ...) |
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| - | [[Image:1m3d.gif|left|200px]]<br /><applet load="1m3d" size=" | + | [[Image:1m3d.gif|left|200px]]<br /><applet load="1m3d" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1m3d, resolution 2.0Å" /> | caption="1m3d, resolution 2.0Å" /> | ||
'''Structure of Type IV Collagen NC1 Domains'''<br /> | '''Structure of Type IV Collagen NC1 Domains'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Type IV collagen, which is present in all metazoan, exists as a family of | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1M3D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with LU, BR and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1M3D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=LU:'>LU</scene>, <scene name='pdbligand=BR:'>BR</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M3D OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Hudson, B | + | [[Category: Hudson, B G.]] |
[[Category: Meiyappan, M.]] | [[Category: Meiyappan, M.]] | ||
[[Category: Sundaramoorthy, M.]] | [[Category: Sundaramoorthy, M.]] | ||
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[[Category: type iv collagen]] | [[Category: type iv collagen]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:06 2008'' |
Revision as of 11:51, 21 February 2008
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Structure of Type IV Collagen NC1 Domains
Overview
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.
About this Structure
1M3D is a Protein complex structure of sequences from Bos taurus with , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of NC1 domains. Structural basis for type IV collagen assembly in basement membranes., Sundaramoorthy M, Meiyappan M, Todd P, Hudson BG, J Biol Chem. 2002 Aug 23;277(34):31142-53. Epub 2002 Apr 22. PMID:11970952
Page seeded by OCA on Thu Feb 21 13:51:06 2008
Categories: Bos taurus | Protein complex | Hudson, B G. | Meiyappan, M. | Sundaramoorthy, M. | Todd, P. | BR | GOL | LU | 3d domain swapping | Basement membrane | Br-mad | Nc1 domain | Network assembly | Type iv collagen
