View source for 4ae2


==Crystal structure of Human fibrillar procollagen type III C- propeptide trimer==
<StructureSection load='4ae2' size='340' side='right'caption='[[4ae2]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ae2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AE2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.68&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ae2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ae2 OCA], [https://pdbe.org/4ae2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ae2 RCSB], [https://www.ebi.ac.uk/pdbsum/4ae2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ae2 ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/CO3A1_HUMAN CO3A1_HUMAN] Defects in COL3A1 are a cause of Ehlers-Danlos syndrome type 3 (EDS3) [MIM:[https://omim.org/entry/130020 130020]; also known as benign hypermobility syndrome. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS3 is a form of Ehlers-Danlos syndrome characterized by marked joint hyperextensibility without skeletal deformity.<ref>PMID:7833919</ref>   Defects in COL3A1 are the cause of Ehlers-Danlos syndrome type 4 (EDS4) [MIM:[https://omim.org/entry/130050 130050]. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS4 is the most severe form of the disease. It is characterized by the joint and dermal manifestations as in other forms of the syndrome, characteristic facial features (acrogeria) in most patients, and by proneness to spontaneous rupture of bowel and large arteries. The vascular complications may affect all anatomical areas.<ref>PMID:1370809</ref> <ref>PMID:8411057</ref> <ref>PMID:2492273</ref> <ref>PMID:7749417</ref> <ref>PMID:1352273</ref> <ref>PMID:2808425</ref> <ref>PMID:1895316</ref> <ref>PMID:1357232</ref> <ref>PMID:1496983</ref> <ref>PMID:8098182</ref> [:]<ref>PMID:7912131</ref> <ref>PMID:8019562</ref> [:]<ref>PMID:8680408</ref> <ref>PMID:8884076</ref> <ref>PMID:9147870</ref> <ref>PMID:8664902</ref> <ref>PMID:8990011</ref> <ref>PMID:9036918</ref> <ref>PMID:9452103</ref> <ref>PMID:10923041</ref> <ref>PMID:10706896</ref> <ref>PMID:11168790</ref> <ref>PMID:12694234</ref> <ref>PMID:12786757</ref>   Defects in COL3A1 are a cause of susceptibility to aortic aneurysm abdominal (AAA) [MIM:[https://omim.org/entry/100070 100070]. AAA is a common multifactorial disorder characterized by permanent dilation of the abdominal aorta, usually due to degenerative changes in the aortic wall. Histologically, AAA is characterized by signs of chronic inflammation, destructive remodeling of the extracellular matrix, and depletion of vascular smooth muscle cells.<ref>PMID:8514866</ref> <ref>PMID:2243125</ref> <ref>PMID:2349939</ref> 
== Function ==
[https://www.uniprot.org/uniprot/CO3A1_HUMAN CO3A1_HUMAN] Collagen type III occurs in most soft connective tissues along with type I collagen.
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== Publication Abstract from PubMed ==
The C propeptides of fibrillar procollagens have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. Mutations in C propeptides are associated with several, often lethal, genetic disorders affecting bone, cartilage, blood vessels and skin. Here we report the crystal structure of a C-propeptide domain from human procollagen III. It reveals an exquisite structural mechanism of chain recognition during intracellular trimerization of the procollagen molecule. It also gives insights into why some types of collagen consist of three identical polypeptide chains, whereas others do not. Finally, the data show striking correlations between the sites of numerous disease-related mutations in different C-propeptide domains and the degree of phenotype severity. The results have broad implications for understanding genetic disorders of connective tissues and designing new therapeutic strategies.

Structural basis of fibrillar collagen trimerization and related genetic disorders.,Bourhis JM, Mariano N, Zhao Y, Harlos K, Exposito JY, Jones EY, Moali C, Aghajari N, Hulmes DJ Nat Struct Mol Biol. 2012 Oct;19(10):1031-6. doi: 10.1038/nsmb.2389. Epub 2012, Sep 23. PMID:23001006<ref>PMID:23001006</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4ae2" style="background-color:#fffaf0;"></div>

==See Also==
*[[Collagen 3D structures|Collagen 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Aghajari N]]
[[Category: Bourhis JM]]
[[Category: Harlos K]]
[[Category: Hulmes DJ]]
[[Category: Jones EY]]
[[Category: Mariano N]]
[[Category: Moali C]]
[[Category: Zhao Y]]