1aq5: Difference between revisions
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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=1aq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aq5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aq5 RCSB], [http://www.ebi.ac.uk/pdbsum/1aq5 PDBsum]</span></td></tr> | <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=1aq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aq5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aq5 RCSB], [http://www.ebi.ac.uk/pdbsum/1aq5 PDBsum]</span></td></tr> | ||
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== Function == | |||
[[http://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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 18:55, 25 December 2014
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
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 PubMedThe 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
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