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{{STRUCTURE_2knt|  PDB=2knt  |  SCENE=  }}
==THE 1.2 ANGSTROM STRUCTURE OF KUNITZ TYPE DOMAIN C5==
===THE 1.2 ANGSTROM STRUCTURE OF KUNITZ TYPE DOMAIN C5===
<StructureSection load='2knt' size='340' side='right' caption='[[2knt]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
{{ABSTRACT_PUBMED_9761897}}
== Structural highlights ==
 
<table><tr><td colspan='2'>[[2knt]] is a 1 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=2KNT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KNT FirstGlance]. <br>
==Disease==
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br>
[[http://www.uniprot.org/uniprot/CO6A3_HUMAN CO6A3_HUMAN]] Defects in COL6A3 are a cause of Bethlem myopathy (BM) [MIM:[http://omim.org/entry/158810 158810]]. BM is a rare autosomal dominant proximal myopathy characterized by early childhood onset (complete penetrance by the age of 5) and joint contractures most frequently affecting the elbows and ankles.<ref>PMID:11992252</ref><ref>PMID:9536084</ref><ref>PMID:10399756</ref><ref>PMID:15689448</ref><ref>PMID:17886299</ref> Defects in COL6A3 are a cause of Ullrich congenital muscular dystrophy (UCMD) [MIM:[http://omim.org/entry/254090 254090]]; also known as Ullrich scleroatonic muscular dystrophy. UCMD is an autosomal recessive congenital myopathy characterized by muscle weakness and multiple joint contractures, generally noted at birth or early infancy. The clinical course is more severe than in Bethlem myopathy.<ref>PMID:11992252</ref><ref>PMID:15689448</ref>  
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2knt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2knt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2knt RCSB], [http://www.ebi.ac.uk/pdbsum/2knt PDBsum]</span></td></tr>
<table>
== Disease ==
[[http://www.uniprot.org/uniprot/CO6A3_HUMAN CO6A3_HUMAN]] Defects in COL6A3 are a cause of Bethlem myopathy (BM) [MIM:[http://omim.org/entry/158810 158810]]. BM is a rare autosomal dominant proximal myopathy characterized by early childhood onset (complete penetrance by the age of 5) and joint contractures most frequently affecting the elbows and ankles.<ref>PMID:11992252</ref> <ref>PMID:9536084</ref> <ref>PMID:10399756</ref> <ref>PMID:15689448</ref> <ref>PMID:17886299</ref>   Defects in COL6A3 are a cause of Ullrich congenital muscular dystrophy (UCMD) [MIM:[http://omim.org/entry/254090 254090]]; also known as Ullrich scleroatonic muscular dystrophy. UCMD is an autosomal recessive congenital myopathy characterized by muscle weakness and multiple joint contractures, generally noted at birth or early infancy. The clinical course is more severe than in Bethlem myopathy.<ref>PMID:11992252</ref> <ref>PMID:15689448</ref>
== Function ==
[[http://www.uniprot.org/uniprot/CO6A3_HUMAN CO6A3_HUMAN]] Collagen VI acts as a cell-binding protein.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kn/2knt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The recombinant Kunitz-type domain (C5) of human collagen alpha3(VI) chain was previously described at 1.6 A resolution at room temperature. By changing the crystallization conditions and using synchrotron radiation, we are able to record diffraction data to 1.2 A resolution for crystals of the same space group at 291 K. The protein-water-ion model has been refined anisotropically against these new data using the program SHELXL93; the results converged to an R factor of 15.0%, with all data between 7 and 1.2 A. The final electron-density map reveals a clear chain tracing with a few disordered residues and five residues out of 58 that present alternate conformations. The Cys14-Cys38 bond presents the less frequently observed left-hand conformation (chi1 = -60 degrees). The solvent molecules and a phosphate ion are well ordered with an average B of 38 A2. The high-resolution structure reveals the N and C termini which were missing from the 1.6 A structure.


==Function==
1.2 A refinement of the Kunitz-type domain from the alpha3 chain of human type VI collagen.,Merigeau K, Arnoux B, Perahia D, Norris K, Norris F, Ducruix A Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):306-12. PMID:9761897<ref>PMID:9761897</ref>
[[http://www.uniprot.org/uniprot/CO6A3_HUMAN CO6A3_HUMAN]] Collagen VI acts as a cell-binding protein.  


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[2knt]] is a 1 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=2KNT OCA].
</div>


==See Also==
==See Also==
*[[Collagen|Collagen]]
*[[Collagen|Collagen]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:009761897</ref><references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Arnoux, B.]]
[[Category: Arnoux, B.]]

Revision as of 12:09, 30 September 2014

THE 1.2 ANGSTROM STRUCTURE OF KUNITZ TYPE DOMAIN C5THE 1.2 ANGSTROM STRUCTURE OF KUNITZ TYPE DOMAIN C5

Structural highlights

2knt is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, RCSB, PDBsum

Disease

[CO6A3_HUMAN] Defects in COL6A3 are a cause of Bethlem myopathy (BM) [MIM:158810]. BM is a rare autosomal dominant proximal myopathy characterized by early childhood onset (complete penetrance by the age of 5) and joint contractures most frequently affecting the elbows and ankles.[1] [2] [3] [4] [5] Defects in COL6A3 are a cause of Ullrich congenital muscular dystrophy (UCMD) [MIM:254090]; also known as Ullrich scleroatonic muscular dystrophy. UCMD is an autosomal recessive congenital myopathy characterized by muscle weakness and multiple joint contractures, generally noted at birth or early infancy. The clinical course is more severe than in Bethlem myopathy.[6] [7]

Function

[CO6A3_HUMAN] Collagen VI acts as a cell-binding protein.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The recombinant Kunitz-type domain (C5) of human collagen alpha3(VI) chain was previously described at 1.6 A resolution at room temperature. By changing the crystallization conditions and using synchrotron radiation, we are able to record diffraction data to 1.2 A resolution for crystals of the same space group at 291 K. The protein-water-ion model has been refined anisotropically against these new data using the program SHELXL93; the results converged to an R factor of 15.0%, with all data between 7 and 1.2 A. The final electron-density map reveals a clear chain tracing with a few disordered residues and five residues out of 58 that present alternate conformations. The Cys14-Cys38 bond presents the less frequently observed left-hand conformation (chi1 = -60 degrees). The solvent molecules and a phosphate ion are well ordered with an average B of 38 A2. The high-resolution structure reveals the N and C termini which were missing from the 1.6 A structure.

1.2 A refinement of the Kunitz-type domain from the alpha3 chain of human type VI collagen.,Merigeau K, Arnoux B, Perahia D, Norris K, Norris F, Ducruix A Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):306-12. PMID:9761897[8]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Demir E, Sabatelli P, Allamand V, Ferreiro A, Moghadaszadeh B, Makrelouf M, Topaloglu H, Echenne B, Merlini L, Guicheney P. Mutations in COL6A3 cause severe and mild phenotypes of Ullrich congenital muscular dystrophy. Am J Hum Genet. 2002 Jun;70(6):1446-58. Epub 2002 Apr 24. PMID:11992252 doi:S0002-9297(07)60697-1
  2. ↑ Pan TC, Zhang RZ, Pericak-Vance MA, Tandan R, Fries T, Stajich JM, Viles K, Vance JM, Chu ML, Speer MC. Missense mutation in a von Willebrand factor type A domain of the alpha 3(VI) collagen gene (COL6A3) in a family with Bethlem myopathy. Hum Mol Genet. 1998 May;7(5):807-12. PMID:9536084
  3. ↑ Pepe G, Bertini E, Giusti B, Brunelli T, Comeglio P, Saitta B, Merlini L, Chu ML, Federici G, Abbate R. A novel de novo mutation in the triple helix of the COL6A3 gene in a two-generation Italian family affected by Bethlem myopathy. A diagnostic approach in the mutations' screening of type VI collagen. Neuromuscul Disord. 1999 Jun;9(4):264-71. PMID:10399756
  4. ↑ Lampe AK, Dunn DM, von Niederhausern AC, Hamil C, Aoyagi A, Laval SH, Marie SK, Chu ML, Swoboda K, Muntoni F, Bonnemann CG, Flanigan KM, Bushby KM, Weiss RB. Automated genomic sequence analysis of the three collagen VI genes: applications to Ullrich congenital muscular dystrophy and Bethlem myopathy. J Med Genet. 2005 Feb;42(2):108-20. PMID:15689448 doi:42/2/108
  5. ↑ Baker NL, Morgelin M, Pace RA, Peat RA, Adams NE, Gardner RJ, Rowland LP, Miller G, De Jonghe P, Ceulemans B, Hannibal MC, Edwards M, Thompson EM, Jacobson R, Quinlivan RC, Aftimos S, Kornberg AJ, North KN, Bateman JF, Lamande SR. Molecular consequences of dominant Bethlem myopathy collagen VI mutations. Ann Neurol. 2007 Oct;62(4):390-405. PMID:17886299 doi:10.1002/ana.21213
  6. ↑ Demir E, Sabatelli P, Allamand V, Ferreiro A, Moghadaszadeh B, Makrelouf M, Topaloglu H, Echenne B, Merlini L, Guicheney P. Mutations in COL6A3 cause severe and mild phenotypes of Ullrich congenital muscular dystrophy. Am J Hum Genet. 2002 Jun;70(6):1446-58. Epub 2002 Apr 24. PMID:11992252 doi:S0002-9297(07)60697-1
  7. ↑ Lampe AK, Dunn DM, von Niederhausern AC, Hamil C, Aoyagi A, Laval SH, Marie SK, Chu ML, Swoboda K, Muntoni F, Bonnemann CG, Flanigan KM, Bushby KM, Weiss RB. Automated genomic sequence analysis of the three collagen VI genes: applications to Ullrich congenital muscular dystrophy and Bethlem myopathy. J Med Genet. 2005 Feb;42(2):108-20. PMID:15689448 doi:42/2/108
  8. ↑ Merigeau K, Arnoux B, Perahia D, Norris K, Norris F, Ducruix A. 1.2 A refinement of the Kunitz-type domain from the alpha3 chain of human type VI collagen. Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):306-12. PMID:9761897

2knt, resolution 1.20Å

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