1cag: Difference between revisions
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'''CRYSTAL AND MOLECULAR STRUCTURE OF A COLLAGEN-LIKE PEPTIDE AT 1.9 ANGSTROM RESOLUTION''' | {{Structure | ||
|PDB= 1cag |SIZE=350|CAPTION= <scene name='initialview01'>1cag</scene>, resolution 1.85Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL AND MOLECULAR STRUCTURE OF A COLLAGEN-LIKE PEPTIDE AT 1.9 ANGSTROM RESOLUTION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CAG is a [ | 1CAG is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. The following page contains interesting information on the relation of 1CAG with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb4_1.html Collagen]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CAG OCA]. | ||
==Reference== | ==Reference== | ||
Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution., Bella J, Eaton M, Brodsky B, Berman HM, Science. 1994 Oct 7;266(5182):75-81. PMID:[http:// | Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution., Bella J, Eaton M, Brodsky B, Berman HM, Science. 1994 Oct 7;266(5182):75-81. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7695699 7695699] | ||
[[Category: Collagen]] | [[Category: Collagen]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: collagen]] | [[Category: collagen]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:22:00 2008'' | ||
Revision as of 11:22, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL AND MOLECULAR STRUCTURE OF A COLLAGEN-LIKE PEPTIDE AT 1.9 ANGSTROM RESOLUTION
OverviewOverview
The structure of a protein triple helix has been determined at 1.9 angstrom resolution by x-ray crystallographic studies of a collagen-like peptide containing a single substitution of the consensus sequence. This peptide adopts a triple-helical structure that confirms the basic features determined from fiber diffraction studies on collagen: supercoiling of polyproline II helices and interchain hydrogen bonding that follows the model II of Rich and Crick. In addition, the structure provides new information concerning the nature of this protein fold. Each triple helix is surrounded by a cylinder of hydration, with an extensive hydrogen bonding network between water molecules and peptide acceptor groups. Hydroxyproline residues have a critical role in this water network. The interaxial spacing of triple helices in the crystal is similar to that in collagen fibrils, and the water networks linking adjacent triple helices in the crystal structure are likely to be present in connective tissues. The breaking of the repeating (X-Y-Gly)n pattern by a Gly-->Ala substitution results in a subtle alteration of the conformation, with a local untwisting of the triple helix. At the substitution site, direct interchain hydrogen bonds are replaced with interstitial water bridges between the peptide groups. Similar conformational changes may occur in Gly-->X mutated collagens responsible for the diseases osteogenesis imperfecta, chondrodysplasias, and Ehlers-Danlos syndrome IV.
About this StructureAbout this Structure
1CAG is a Protein complex structure of sequences from [1]. The following page contains interesting information on the relation of 1CAG with [Collagen]. Full crystallographic information is available from OCA.
ReferenceReference
Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution., Bella J, Eaton M, Brodsky B, Berman HM, Science. 1994 Oct 7;266(5182):75-81. PMID:7695699
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