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Collagen: Difference between revisions

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The <scene name='Collagen/1cag_surface/4'>surface</scene> of the tropocollagen is shown with the Ala appearing as olive and the Pro and Hyp adjacent to the Ala appearing as dark brown.  Notice that the surface at these Pro and Hyp bulges slightly.  This protrusion is due to the fact that the packing about the Ala side chains is not as close as it is about the Gly.  In the two side-by-side scenes shown below compare the amount of open space between the chains in the area of the scene center.  In the [[1cag]] scene in the area of the Ala the distance between the chains is slightly greater than that of [[4clg]] scene.  
The <scene name='Collagen/1cag_surface/4'>surface</scene> of the tropocollagen is shown with the Ala appearing as olive and the Pro and Hyp adjacent to the Ala appearing as dark brown.  Notice that the surface at these Pro and Hyp bulges slightly.  This protrusion is due to the fact that the packing about the Ala side chains is not as close as it is about the Gly.  In the two side-by-side scenes shown below compare the amount of open space between the chains in the area of the scene center.  In the [[1cag]] scene in the area of the Ala the distance between the chains is slightly greater than that of [[4clg]] scene.  


==3D structures of collagen==
[[Collagen 3D structures]]


</StructureSection>
</StructureSection>
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In order to convince yourself that there is a difference in the interchain distances in the area of the Ala, <scene name='Collagen/1cag_measurements/2'>show distances</scene> between Gly (Ala) and Pro which form intratropocollagen hydrogen bonds.  Hydrogen bonds are not formed between Ala and Pro because the distances between the atoms forming the bonds are too great.  The absence of the intratropocollagen hydrogen bonds, which is due to replacing Gly with a residue having a longer side chain, disrupts collagen's rope-like structure and is responsible for the symptoms of such human diseases as osteogenesis imperfecta and certain Ehlers-Danlos syndromes.
In order to convince yourself that there is a difference in the interchain distances in the area of the Ala, <scene name='Collagen/1cag_measurements/2'>show distances</scene> between Gly (Ala) and Pro which form intratropocollagen hydrogen bonds.  Hydrogen bonds are not formed between Ala and Pro because the distances between the atoms forming the bonds are too great.  The absence of the intratropocollagen hydrogen bonds, which is due to replacing Gly with a residue having a longer side chain, disrupts collagen's rope-like structure and is responsible for the symptoms of such human diseases as osteogenesis imperfecta and certain Ehlers-Danlos syndromes.
==3D structures of collagen==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
* Collagen
**[[3hqv]], [[3hr2]] – Col I – rat – fiber diffraction<br />
**[[1q7d]] - hCol I α1 integrin-binding domain – human<br />
**[[2llp]] - hCol I α1 fragment – NMR<br />
**[[1u5m]] - hCol II α1 (mutant) <br /> 
**[[3dmw]] - hCol III α1residues 1158-1199 (mutant)<br />
**[[4ae2]] - hCol III residues 1222-1466<br />
**[[4aej]], [[4ak3]] - hCol III residues 1222-1466 (mutant)<br />
**[[1kth]] - hCol III α3 Kunitz type domain<br />
**[[1kun]] - hCol III α3 Kunitz type domain – NMR<BR />
**[[1li1]] - hCol IV α Nc1 domain<br />
**[[1t60]], [[1t61]], [[1m3d]] - Col IV α Nc1 domain – bovine<br />
**[[2knt]], [[1knt]] - hCol VI  Kunitz type domain<br />
**[[4igi]] - mCol VI α3 N5 domain – mouse<br />
**[[4ihk]] - mCol VI α3 N5 domain (mutant)<br />
**[[1o91]] - mCol VIII α1 Nc1 domain <br />
**[[2uur]] - hCol IX α1 Nc4 domain<br />
**[[1b9p]], [[1b9q]] - Col IX α1 Nc4 domain (mutant) <br />
**[[5cvb]], [[5cva]], [[5cti]], [[5ctd]] - Col IX α1+ α2+ α3<br />
**[[1gr3]] - hCol X α1 Nc1 domain<br />
**[[3n3f]] – hCol XIV Nc1 domain<br />
**[[1dy2]] - mCol XV endostatin domain<br />
**[[3hon]], [[3hsh]] - hCol XVIII tetramerization domain<br />
**[[1bnl]] - hCol XVIII C terminal domain<br />
**[[1dy0]], [[1dy1]] - mCol XVIII endostatin domain<br />
**[[2ekj]], [[2ee3]], [[5kf4]] - hCol XX α1 fn3 domain<br />
**[[2dkm]] - hCol XX α1 fn3 domain - NMR<BR />
**[[3ipn]] – Col modified<br />
**[[1wzb]], [[1itt]], [[1k6f]], [[1ym8]] – Col triple helix<br />
**[[1zpx]], [[1sp7]], [[1sop]] – Col mini – hydra – NMR<BR />
**[[2cuo]], [[2d3f]], [[2d3h]], [[2g66]] – Col model peptides
*Collagen complex with binding proteins
**[[3ejh]], [[3gxe]] – hCol I α1 C-terminal + fibronectin<br />
**[[2fse]] – hCol II + MHC HLA-DR1<br />
**[[2seb]] - hCol II + MHC HLA-DR4<br />
**[[2v53]] - hCol III α1 + Sparc<br />
**[[2wuh]] – hCol + discoidin domain receptor 2<br />
**[[1dzi]] – Col + integrin α2 domain<br />
**[[2f6a]] – Col + Col adhesin
}}


==References==
==References==

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Ala Jelani, Karl Oberholser, Eran Hodis, Tilman Schirmer, Judy Voet, David Canner, Jaime Prilusky, Michal Harel, Alexander Berchansky, Eric Martz
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