1k94
From Proteopedia
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| - | [[Image:1k94.jpg|left|200px]] | + | [[Image:1k94.jpg|left|200px]] |
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| - | '''Crystal structure of des(1-52)grancalcin with bound calcium''' | + | {{Structure |
| + | |PDB= 1k94 |SIZE=350|CAPTION= <scene name='initialview01'>1k94</scene>, resolution 1.70Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Crystal structure of des(1-52)grancalcin with bound calcium''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1K94 is a [ | + | 1K94 is a [[Single protein]] structure of 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=1K94 OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of Ca(2+)-loaded human grancalcin., Jia J, Borregaard N, Lollike K, Cygler M, Acta Crystallogr D Biol Crystallogr. 2001 Dec;57(Pt 12):1843-9. Epub 2001, Nov 21. PMID:[http:// | + | Structure of Ca(2+)-loaded human grancalcin., Jia J, Borregaard N, Lollike K, Cygler M, Acta Crystallogr D Biol Crystallogr. 2001 Dec;57(Pt 12):1843-9. Epub 2001, Nov 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11717497 11717497] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: penta-ef-hand protein]] | [[Category: penta-ef-hand protein]] | ||
| - | ''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 12:14:11 2008'' |
Revision as of 10:14, 20 March 2008
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| , resolution 1.70Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of des(1-52)grancalcin with bound calcium
Contents |
Overview
Grancalcin is a cytosolic Ca(2+)-binding protein originally identified in human neutrophils. It belongs to a new class of EF-hand proteins, called PEF proteins, which contain five EF-hand motifs. At the N-terminus of grancalcin there is a approximately 50 residue-long segment rich in glycines and prolines. The fifth EF-hand, unpaired within the monomer, provides a means for dimerization through pairing with its counterpart in a second molecule. The structure of full-length grancalcin in the apo form and with one EF3 within the dimer occupied by a Ca(2+) ion have been determined. Although the N-terminal segment was present in the molecule, this part was disordered in the crystals. Here, the structure of a truncated form of grancalcin, which is lacking 52 N-terminal residues, in the presence and absence of Ca(2+) is presented. In the Ca(2+)-bound form the ions are found in the EF1 and EF3 hands. Binding of Ca(2+) to these two EF hands produces only minor conformational changes, mostly within the EF1 Ca(2+)-binding loop. This observation supports the hypothesis, formulated on the basis of the structure of a homologous protein ALG-2 which shows significant differences in the orientation of EF4 and EF5 compared with grancalcin, that calcium is a necessary factor but not sufficient alone for inducing a significant conformational change in PEF proteins.
Disease
Known diseases associated with this structure: Cone dystrophy-3 OMIM:[600364], Hemolytic anemia due to gamma-glutamylcysteine synthetase deficiency OMIM:[606857]
About this Structure
1K94 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of Ca(2+)-loaded human grancalcin., Jia J, Borregaard N, Lollike K, Cygler M, Acta Crystallogr D Biol Crystallogr. 2001 Dec;57(Pt 12):1843-9. Epub 2001, Nov 21. PMID:11717497
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