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| | {{STRUCTURE_1q3m| PDB=1q3m | SCENE= }} | | {{STRUCTURE_1q3m| PDB=1q3m | SCENE= }} |
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| - | '''1H NMR structure bundle of bovine Ca2+-osteocalcin'''
| + | ===1H NMR structure bundle of bovine Ca2+-osteocalcin=== |
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| - | ==Overview==
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| - | Structural information on osteocalcin or other noncollagenous bone proteins is very limited. We have solved the three-dimensional structure of calcium bound osteocalcin using (1)H 2D NMR techniques and proposed a mechanism for mineral binding. The protons in the 49 amino acid sequence were assigned using standard two-dimensional homonuclear NMR experiments. Distance constraints, dihedral angle constraints, hydrogen bonds, and (1)H and (13)C chemical shifts were all used to calculate a family of 13 structures. The tertiary structure of the protein consisted of an unstructured N terminus and a C-terminal loop (residues 16-49) formed by long-range hydrophobic interactions. Elements of secondary structure within residues 16-49 include type III turns (residues 20-25) and two alpha-helical regions (residues 27-35 and 41-44). The three Gla residues project from the same face of the helical turns and are surface exposed. The genetic algorithm-molecular dynamics simulation approach was used to place three calcium atoms on the NMR-derived structure. One calcium atom was coordinated by three side chain oxygen atoms, two from Asp30, and one from Gla24. The second calcium atom was coordinated to four oxygen atoms, two from the side chain in Gla 24, and two from the side chain of Gla 21. The third calcium atom was coordinated to two oxygen atoms of the side chain of Gla17. The best correlation of the distances between the uncoordinated Gla oxygen atoms is with the intercalcium distance of 9.43 A in hydroxyapatite. The structure may provide further insight into the function of osteocalcin.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12820886}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12820886 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12820886}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1Q3M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q3M OCA]. | + | 1Q3M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q3M OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Bone protein]] | | [[Category: Bone protein]] |
| | [[Category: Calcium binding protein]] | | [[Category: Calcium binding protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:49:37 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:37:10 2008'' |
Revision as of 02:37, 28 July 2008
Template:STRUCTURE 1q3m
1H NMR structure bundle of bovine Ca2+-osteocalcin
Template:ABSTRACT PUBMED 12820886
About this Structure
1Q3M is a Single protein structure of sequence from Bos taurus. Full experimental information is available from OCA.
Reference
The three-dimensional structure of bovine calcium ion-bound osteocalcin using 1H NMR spectroscopy., Dowd TL, Rosen JF, Li L, Gundberg CM, Biochemistry. 2003 Jul 1;42(25):7769-79. PMID:12820886
Page seeded by OCA on Mon Jul 28 05:37:10 2008
