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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. |
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| ==3D structures of collagen==
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| Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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| {{#tree:id=OrganizedByTopic|openlevels=0|
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| * Collagen
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| **[[3hqv]], [[3hr2]] – Col I – rat – fiber diffraction<br />
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| **[[5k31]] - hCol I 1 residues 1219-1464 - human<br />
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| **[[5nir]] - hCol II 1 VWC domain residues 29-98<br />
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| **[[1u5m]] - hCol II α1 (mutant) <br />
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| **[[3dmw]] - hCol III α1residues 1158-1199 (mutant)<br />
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| **[[4ae2]] - hCol III residues 1222-1466<br />
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| **[[4aej]], [[4ak3]] - hCol III residues 1222-1466 (mutant)<br />
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| **[[1kth]] - hCol III α3 Kunitz type domain<br />
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| **[[1kun]] - hCol III α3 Kunitz type domain – NMR<BR />
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| **[[1li1]] - hCol IV α Nc1 domain<br />
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| **[[1t60]], [[1t61]], [[1m3d]] - Col IV α Nc1 domain – bovine<br />
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| **[[2knt]], [[1knt]] - hCol VI Kunitz type domain<br />
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| **[[4igi]] - mCol VI α3 N5 domain – mouse<br />
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| **[[4ihk]] - mCol VI α3 N5 domain (mutant)<br />
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| **[[1o91]] - mCol VIII α1 Nc1 domain <br />
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| **[[2uur]] - hCol IX α1 Nc4 domain<br />
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| **[[1b9p]], [[1b9q]] - Col IX α1 Nc4 domain (mutant) <br />
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| **[[5cvb]], [[5cva]], [[5cti]], [[5ctd]] - Col IX α1+ α2+ α3<br />
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| **[[1gr3]] - hCol X α1 Nc1 domain<br />
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| **[[3n3f]] – hCol XIV Nc1 domain<br />
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| **[[1dy2]] - mCol XV endostatin domain<br />
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| **[[3hon]], [[3hsh]] - hCol XVIII tetramerization domain<br />
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| **[[1bnl]] - hCol XVIII C terminal domain<br />
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| **[[1dy0]], [[1dy1]] - mCol XVIII endostatin domain<br />
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| **[[2ekj]], [[2ee3]], [[5kf4]] - hCol XX α1 fn3 domain<br />
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| **[[2dkm]] - hCol XX α1 fn3 domain - NMR<BR />
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| **[[3ipn]] – Col modified<br />
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| **[[1wzb]], [[1itt]], [[1k6f]], [[1ym8]] – Col triple helix<br />
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| **[[1zpx]], [[1sp7]], [[1sop]] – Col mini – hydra – NMR<BR />
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| **[[2cuo]], [[2d3f]], [[2d3h]], [[2g66]] – Col model peptides
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| *Collagen complex with binding proteins
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| **[[3ejh]], [[3gxe]] – hCol I α1 C-terminal + fibronectin<br />
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| **[[2fse]] – hCol II + MHC HLA-DR1<br />
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| **[[2seb]] - hCol II + MHC HLA-DR4<br />
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| **[[2v53]] - hCol III α1 + Sparc<br />
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| **[[2wuh]] – hCol + discoidin domain receptor 2<br />
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| **[[1dzi]] – Col + integrin α2 domain<br />
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| **[[2f6a]] – Col + Col adhesin
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| }}
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| ==References== | | ==References== |