2v53

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{{STRUCTURE_2v53| PDB=2v53 | SCENE= }}
 
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===CRYSTAL STRUCTURE OF A SPARC-COLLAGEN COMPLEX===
 
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{{ABSTRACT_PUBMED_19011090}}
 
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==Disease==
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==Crystal structure of a SPARC-collagen complex==
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[[http://www.uniprot.org/uniprot/CO3A1_HUMAN CO3A1_HUMAN]] Defects in COL3A1 are a cause of Ehlers-Danlos syndrome type 3 (EDS3) [MIM:[http://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:[http://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:[http://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>
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<StructureSection load='2v53' size='340' side='right'caption='[[2v53]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2v53]] is a 4 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=2V53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V53 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
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<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=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v53 OCA], [https://pdbe.org/2v53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v53 RCSB], [https://www.ebi.ac.uk/pdbsum/2v53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v53 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SPRC_HUMAN SPRC_HUMAN] Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Protein interactions with the collagen triple helix play a critical role in collagen fibril formation, cell adhesion, and signaling. However, structural insight into sequence-specific collagen recognition is limited to an integrin-peptide complex. A GVMGFO motif in fibrillar collagens (O denotes 4-hydroxyproline) binds 3 unrelated proteins: von Willebrand factor (VWF), discoidin domain receptor 2 (DDR2), and the extracellular matrix protein SPARC/osteonectin/BM-40. We report the crystal structure at 3.2 A resolution of human SPARC bound to a triple-helical 33-residue peptide harboring the promiscuous GVMGFO motif. SPARC recognizes the GVMGFO motifs of the middle and trailing collagen chains, burying a total of 720 A(2) of solvent-accessible collagen surface. SPARC binding does not distort the canonical triple helix of the collagen peptide. In contrast, a critical loop in SPARC is substantially remodelled upon collagen binding, creating a deep pocket that accommodates the phenylalanine residue of the trailing collagen chain ("Phe pocket"). This highly restrictive specificity pocket is shared with the collagen-binding integrin I-domains but differs strikingly from the shallow collagen-binding grooves of the platelet receptor glycoprotein VI and microbial adhesins. We speculate that binding of the GVMGFO motif to VWF and DDR2 also results in structural changes and the formation of a Phe pocket.
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==Function==
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Structural basis of sequence-specific collagen recognition by SPARC.,Hohenester E, Sasaki T, Giudici C, Farndale RW, Bachinger HP Proc Natl Acad Sci U S A. 2008 Nov 25;105(47):18273-7. Epub 2008 Nov 14. PMID:19011090<ref>PMID:19011090</ref>
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[[http://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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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[2v53]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V53 OCA].
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</div>
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<div class="pdbe-citations 2v53" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Collagen|Collagen]]
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*[[Collagen 3D structures|Collagen 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:019011090</ref><ref group="xtra">PMID:009501084</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Bachinger, H P.]]
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[[Category: Large Structures]]
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[[Category: Farndale, R W.]]
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[[Category: Bachinger HP]]
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[[Category: Giudici, C.]]
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[[Category: Farndale RW]]
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[[Category: Hohenester, E.]]
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[[Category: Giudici C]]
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[[Category: Sasaki, T.]]
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[[Category: Hohenester E]]
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[[Category: Basement membrane]]
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[[Category: Sasaki T]]
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[[Category: Cell adhesion]]
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[[Category: Collagen]]
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[[Category: Extracellular matrix]]
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[[Category: Glycoprotein]]
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[[Category: Glycosylated protein]]
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[[Category: Ion transport]]
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[[Category: Ionic channel]]
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[[Category: Secreted]]
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[[Category: Transport]]
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Current revision

Crystal structure of a SPARC-collagen complex

PDB ID 2v53

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