View source for 3dmw


==Crystal structure of human type III collagen G982-G1023 containing C-terminal cystine knot==
<StructureSection load='3dmw' size='340' side='right'caption='[[3dmw]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3dmw]] 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=3DMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DMW 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3dmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dmw OCA], [https://pdbe.org/3dmw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dmw RCSB], [https://www.ebi.ac.uk/pdbsum/3dmw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dmw 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Type III collagen is a critical collagen that comprises extensible connective tissue such as skin, lung, and the vascular system. Mutations in the type III collagen gene, COL3A1, are associated with the most severe forms of Ehlers-Danlos syndrome. A characteristic feature of type III collagen is the presence of a stabilizing C-terminal cystine knot. Crystal structures of collagen triple helices reported so far contain artificial sequences like (Gly-Pro-Pro)(n) or (Gly-Pro-Hyp)(n). To gain insight into the structural properties exhibited by the natural type III collagen triple helix, we synthesized, crystallized, and determined the structure of a 12-triplet repeating peptide containing the natural type III collagen sequence from residues 991 to 1032 including the C-terminal cystine knot region, to 2.3A resolution. This represents the longest collagen triple helical structure determined to date with a native sequence. Strikingly, the Gly(991)-Gly(1032) structure reveals that the central non-imino acid-containing region adopts 10/3 superhelical properties, whereas the imino acid rich N- and C-terminal regions adhere to a 7/2 superhelical conformation. The structure is consistent with two models for the cystine knot; however, the poor density for the majority of this region suggests that multiple conformations may be adopted. The structure shows that the multiple non-imino acids make several types of direct intrahelical as well as interhelical contacts. The looser superhelical structure of the non-imino acid region of collagen triple helices combined with the extra contacts afforded by ionic and polar residues likely play a role in fibrillar assembly and interactions with other extracellular components.

Crystal structure of human type III collagen Gly991-Gly1032 cystine knot-containing peptide shows both 7/2 and 10/3 triple helical symmetries.,Boudko SP, Engel J, Okuyama K, Mizuno K, Bachinger HP, Schumacher MA J Biol Chem. 2008 Nov 21;283(47):32580-9. Epub 2008 Sep 19. PMID:18805790<ref>PMID:18805790</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3dmw" style="background-color:#fffaf0;"></div>

==See Also==
*[[Collagen 3D structures|Collagen 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bachinger HP]]
[[Category: Boudko SP]]
[[Category: Engel J]]
[[Category: Mizuno K]]
[[Category: Okuyama K]]
[[Category: Schumacher MA]]