5nv6

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==Structure of human transforming growth factor beta-induced protein (TGFBIp).==
==Structure of human transforming growth factor beta-induced protein (TGFBIp).==
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<StructureSection load='5nv6' size='340' side='right' caption='[[5nv6]], [[Resolution|resolution]] 2.93&Aring;' scene=''>
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<StructureSection load='5nv6' size='340' side='right'caption='[[5nv6]], [[Resolution|resolution]] 2.93&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5nv6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NV6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NV6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5nv6]] is a 2 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=5NV6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NV6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
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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]] 2.93&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5nv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nv6 OCA], [http://pdbe.org/5nv6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nv6 RCSB], [http://www.ebi.ac.uk/pdbsum/5nv6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nv6 ProSAT]</span></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=ACT:ACETATE+ION'>ACT</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=5nv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nv6 OCA], [https://pdbe.org/5nv6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nv6 RCSB], [https://www.ebi.ac.uk/pdbsum/5nv6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nv6 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/BGH3_HUMAN BGH3_HUMAN]] Defects in TGFBI are the cause of epithelial basement membrane corneal dystrophy (EBMD) [MIM:[http://omim.org/entry/121820 121820]]; also known as Cogan corneal dystrophy or map-dot-fingerprint type corneal dystrophy. EBMD is a bilateral anterior corneal dystrophy characterized by grayish epithelial fingerprint lines, geographic map-like lines, and dots (or microcysts) on slit-lamp examination. Pathologic studies show abnormal, redundant basement membrane and intraepithelial lacunae filled with cellular debris. Although this disorder usually is not considered to be inherited, families with autosomal dominant inheritance have been identified.<ref>PMID:16652336</ref> Defects in TGFBI are the cause of corneal dystrophy Groenouw type 1 (CDGG1) [MIM:[http://omim.org/entry/121900 121900]]; also known as corneal dystrophy granular type. Inheritance is autosomal dominant. Corneal dystrophies show progressive opacification of the cornea leading to severe visual handicap.<ref>PMID:15623763</ref> Defects in TGFBI are the cause of corneal dystrophy lattice type 1 (CDL1) [MIM:[http://omim.org/entry/122200 122200]]. Inheritance is autosomal dominant. Defects in TGFBI are a cause of corneal dystrophy Thiel-Behnke type (CDTB) [MIM:[http://omim.org/entry/602082 602082]]; also known as corneal dystrophy of Bowman layer type 2 (CDB2). Defects in TGFBI are the cause of Reis-Buecklers corneal dystrophy (CDRB) [MIM:[http://omim.org/entry/608470 608470]]; also known as corneal dystrophy of Bowman layer type 1 (CDB1).<ref>PMID:15623763</ref> <ref>PMID:9780098</ref> <ref>PMID:10660331</ref> Defects in TGFBI are the cause of lattice corneal dystrophy type 3A (CDL3A) [MIM:[http://omim.org/entry/608471 608471]]. CDL3A clinically resembles to lattice corneal dystrophy type 3, but differs in that its age of onset is 70 to 90 years. It has an autosomal dominant inheritance pattern.<ref>PMID:9497262</ref> <ref>PMID:15790870</ref> Defects in TGFBI are the cause of Avellino corneal dystrophy (ACD) [MIM:[http://omim.org/entry/607541 607541]]. ACD could be considered a variant of granular dystrophy with a significant amyloidogenic tendency. Inheritance is autosomal dominant.
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[https://www.uniprot.org/uniprot/BGH3_HUMAN BGH3_HUMAN] Defects in TGFBI are the cause of epithelial basement membrane corneal dystrophy (EBMD) [MIM:[https://omim.org/entry/121820 121820]; also known as Cogan corneal dystrophy or map-dot-fingerprint type corneal dystrophy. EBMD is a bilateral anterior corneal dystrophy characterized by grayish epithelial fingerprint lines, geographic map-like lines, and dots (or microcysts) on slit-lamp examination. Pathologic studies show abnormal, redundant basement membrane and intraepithelial lacunae filled with cellular debris. Although this disorder usually is not considered to be inherited, families with autosomal dominant inheritance have been identified.<ref>PMID:16652336</ref> Defects in TGFBI are the cause of corneal dystrophy Groenouw type 1 (CDGG1) [MIM:[https://omim.org/entry/121900 121900]; also known as corneal dystrophy granular type. Inheritance is autosomal dominant. Corneal dystrophies show progressive opacification of the cornea leading to severe visual handicap.<ref>PMID:15623763</ref> Defects in TGFBI are the cause of corneal dystrophy lattice type 1 (CDL1) [MIM:[https://omim.org/entry/122200 122200]. Inheritance is autosomal dominant. Defects in TGFBI are a cause of corneal dystrophy Thiel-Behnke type (CDTB) [MIM:[https://omim.org/entry/602082 602082]; also known as corneal dystrophy of Bowman layer type 2 (CDB2). Defects in TGFBI are the cause of Reis-Buecklers corneal dystrophy (CDRB) [MIM:[https://omim.org/entry/608470 608470]; also known as corneal dystrophy of Bowman layer type 1 (CDB1).<ref>PMID:15623763</ref> <ref>PMID:9780098</ref> <ref>PMID:10660331</ref> Defects in TGFBI are the cause of lattice corneal dystrophy type 3A (CDL3A) [MIM:[https://omim.org/entry/608471 608471]. CDL3A clinically resembles to lattice corneal dystrophy type 3, but differs in that its age of onset is 70 to 90 years. It has an autosomal dominant inheritance pattern.<ref>PMID:9497262</ref> <ref>PMID:15790870</ref> Defects in TGFBI are the cause of Avellino corneal dystrophy (ACD) [MIM:[https://omim.org/entry/607541 607541]. ACD could be considered a variant of granular dystrophy with a significant amyloidogenic tendency. Inheritance is autosomal dominant.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/BGH3_HUMAN BGH3_HUMAN]] Binds to type I, II, and IV collagens. This adhesion protein may play an important role in cell-collagen interactions. In cartilage, may be involved in endochondral bone formation.
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[https://www.uniprot.org/uniprot/BGH3_HUMAN BGH3_HUMAN] Binds to type I, II, and IV collagens. This adhesion protein may play an important role in cell-collagen interactions. In cartilage, may be involved in endochondral bone formation.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A major cause of visual impairment, corneal dystrophies result from accumulation of protein deposits in the cornea. One of the proteins involved is transforming growth factor beta-induced protein (TGFBIp), an extracellular matrix component that interacts with integrins but also produces corneal deposits when mutated. Human TGFBIp is a multi-domain 683-residue protein, which contains one CROPT domain and four FAS1 domains. Its structure spans approximately 120 A and reveals that vicinal domains FAS1-1/FAS1-2 and FAS1-3/FAS1-4 tightly interact in an equivalent manner. The FAS1 domains are sandwiches of two orthogonal four-stranded beta sheets decorated with two three-helix insertions. The N-terminal FAS1 dimer forms a compact moiety with the structurally novel CROPT domain, which is a five-stranded all-beta cysteine-knot solely found in TGFBIp and periostin. The overall TGFBIp architecture discloses regions for integrin binding and that most dystrophic mutations cluster at both molecule ends, within domains FAS1-1 and FAS1-4.
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Structural and Functional Implications of Human Transforming Growth Factor beta-Induced Protein, TGFBIp, in Corneal Dystrophies.,Garcia-Castellanos R, Nielsen NS, Runager K, Thogersen IB, Lukassen MV, Poulsen ET, Goulas T, Enghild JJ, Gomis-Ruth FX Structure. 2017 Sep 27. pii: S0969-2126(17)30292-7. doi:, 10.1016/j.str.2017.09.001. PMID:28988748<ref>PMID:28988748</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5nv6" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Enghild, J J]]
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[[Category: Homo sapiens]]
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[[Category: Garcia-Castellanos, R]]
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[[Category: Large Structures]]
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[[Category: Gomis-Ruth, F X]]
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[[Category: Enghild JJ]]
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[[Category: Goulas, T]]
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[[Category: Garcia-Castellanos R]]
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[[Category: Nielsen, S N]]
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[[Category: Gomis-Ruth FX]]
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[[Category: Runager, K]]
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[[Category: Goulas T]]
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[[Category: Thogersen, B I]]
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[[Category: Nielsen SN]]
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[[Category: Structural protein]]
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[[Category: Runager K]]
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[[Category: Thogersen BI]]

Current revision

Structure of human transforming growth factor beta-induced protein (TGFBIp).

PDB ID 5nv6

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