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[[Image:1aq5.gif|left|200px]]


{{Structure
==HIGH-RESOLUTION SOLUTION NMR STRUCTURE OF THE TRIMERIC COILED-COIL DOMAIN OF CHICKEN CARTILAGE MATRIX PROTEIN, 20 STRUCTURES==
|PDB= 1aq5 |SIZE=350|CAPTION= <scene name='initialview01'>1aq5</scene>
<StructureSection load='1aq5' size='340' side='right'caption='[[1aq5]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1aq5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AQ5 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
|GENE= CMP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aq5 OCA], [https://pdbe.org/1aq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aq5 RCSB], [https://www.ebi.ac.uk/pdbsum/1aq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aq5 ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aq5 OCA], [http://www.ebi.ac.uk/pdbsum/1aq5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aq5 RCSB]</span>
[https://www.uniprot.org/uniprot/MATN1_CHICK MATN1_CHICK] Cartilage matrix protein is a major component of the extracellular matrix of non-articular cartilage. It binds to collagen.
}}
== 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/aq/1aq5_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=1aq5 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The solution structure of the oligomerization domain of cartilage matrix protein (also known as matrilin-1) has been determined by heteronuclear NMR spectroscopy. The domain folds into a parallel, disulfide-linked, three-stranded, alpha-helical coiled coil, spanning five heptad repeats in the amino acid sequence. The sequence of the first two heptad repeats shows some deviations from the consensus of hydrophobic and hydrophilic residue preferences. While the corresponding region of the coiled coil has a higher intrinsic flexibility, backbone alpha-helix and superhelix parameters are consistent with a regular coiled coil structure.


'''HIGH-RESOLUTION SOLUTION NMR STRUCTURE OF THE TRIMERIC COILED-COIL DOMAIN OF CHICKEN CARTILAGE MATRIX PROTEIN, 20 STRUCTURES'''
NMR structure of a parallel homotrimeric coiled coil.,Dames SA, Kammerer RA, Wiltscheck R, Engel J, Alexandrescu AT Nat Struct Biol. 1998 Aug;5(8):687-91. PMID:9699631<ref>PMID:9699631</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
==Overview==
</div>
The C-terminal oligomerization domain of chicken cartilage matrix protein is a trimeric coiled coil comprised of three identical 43-residue chains. NMR spectra of the protein show equivalent magnetic environments for each monomer, indicating a parallel coiled coil structure with complete threefold symmetry. Sequence-specific assignments for 1H-, 15N-, and 13C-NMR resonances have been obtained from 2D 1H NOESY and TOCSY spectra, and from 3D HNCA, 15N NOESY-HSQC, and HCCH-TOCSY spectra. A stretch of alpha-helix encompassing five heptad repeats (35 residues) has been identified from intra-chain HN-HN and HN-H alpha NOE connectivities. 3JHNH alpha coupling constants, and chemical shift indices. The alpha-helix begins immediately downstream of inter-chain disulfide bonds between residues Cys 5 and Cys 7, and extends to near the C-terminus of the molecule. The threefold symmetry of the molecule is maintained when the inter-chain disulfide bonds that flank the N-terminus of the coiled coil are reduced. Residues Ile 21 through Glu 36 show conserved chemical shifts and NOE connectivities, as well as strong protection from solvent exchange in the oxidized and reduced forms of the protein. By contrast, residues Ile 10 through Val 17 show pronounced chemical shift differences between the oxidized and reduced protein. Strong chemical exchange NOEs between HN resonances and water indicate solvent exchange on time scales faster than 10 s, and suggests a dynamic fraying of the N-terminus of the coiled coil upon reduction of the disulfide bonds. Possible roles for the disulfide crosslinks of the oligomerization domain in the function of cartilage matrix protein are proposed.
<div class="pdbe-citations 1aq5" style="background-color:#fffaf0;"></div>
 
== References ==
==About this Structure==
<references/>
1AQ5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQ5 OCA].
__TOC__
 
</StructureSection>
==Reference==
Heteronuclear NMR assignments and secondary structure of the coiled coil trimerization domain from cartilage matrix protein in oxidized and reduced forms., Wiltscheck R, Kammerer RA, Dames SA, Schulthess T, Blommers MJ, Engel J, Alexandrescu AT, Protein Sci. 1997 Aug;6(8):1734-45. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9260286 9260286]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Alexandrescu, A T.]]
[[Category: Alexandrescu AT]]
[[Category: Dames, S A.]]
[[Category: Dames SA]]
[[Category: Engel, J.]]
[[Category: Engel J]]
[[Category: Kammerer, R A.]]
[[Category: Kammerer RA]]
[[Category: Wiltscheck, R.]]
[[Category: Wiltscheck R]]
[[Category: cartilage matrix protein]]
[[Category: coiled-coil]]
[[Category: heptad repeat]]
[[Category: interchain disulfide bond]]
[[Category: matrilin-1]]
[[Category: noncollagenous extracellular protein]]
[[Category: oligomerization domain]]
[[Category: trimer]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:45:20 2008''

Latest revision as of 11:20, 6 November 2024

HIGH-RESOLUTION SOLUTION NMR STRUCTURE OF THE TRIMERIC COILED-COIL DOMAIN OF CHICKEN CARTILAGE MATRIX PROTEIN, 20 STRUCTURESHIGH-RESOLUTION SOLUTION NMR STRUCTURE OF THE TRIMERIC COILED-COIL DOMAIN OF CHICKEN CARTILAGE MATRIX PROTEIN, 20 STRUCTURES

Structural highlights

1aq5 is a 3 chain structure with sequence from Gallus gallus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 20 models
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MATN1_CHICK Cartilage matrix protein is a major component of the extracellular matrix of non-articular cartilage. It binds to collagen.

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 solution structure of the oligomerization domain of cartilage matrix protein (also known as matrilin-1) has been determined by heteronuclear NMR spectroscopy. The domain folds into a parallel, disulfide-linked, three-stranded, alpha-helical coiled coil, spanning five heptad repeats in the amino acid sequence. The sequence of the first two heptad repeats shows some deviations from the consensus of hydrophobic and hydrophilic residue preferences. While the corresponding region of the coiled coil has a higher intrinsic flexibility, backbone alpha-helix and superhelix parameters are consistent with a regular coiled coil structure.

NMR structure of a parallel homotrimeric coiled coil.,Dames SA, Kammerer RA, Wiltscheck R, Engel J, Alexandrescu AT Nat Struct Biol. 1998 Aug;5(8):687-91. PMID:9699631[1]

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

References

  1. ↑ Dames SA, Kammerer RA, Wiltscheck R, Engel J, Alexandrescu AT. NMR structure of a parallel homotrimeric coiled coil. Nat Struct Biol. 1998 Aug;5(8):687-91. PMID:9699631 doi:10.1038/1382
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