1nkf: Difference between revisions
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[[Image:1nkf.gif|left|200px]]< | [[Image:1nkf.gif|left|200px]] | ||
'''CALCIUM-BINDING PEPTIDE, NMR, 30 STRUCTURES''' | {{Structure | ||
|PDB= 1nkf |SIZE=350|CAPTION= <scene name='initialview01'>1nkf</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> and <scene name='pdbligand=LA:LANTHANUM (III) ION'>LA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CALCIUM-BINDING PEPTIDE, NMR, 30 STRUCTURES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1NKF is a [ | 1NKF 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=1NKF OCA]. | ||
==Reference== | ==Reference== | ||
Alpha-helix nucleation by a calcium-binding peptide loop., Siedlecka M, Goch G, Ejchart A, Sticht H, Bierzyski A, Proc Natl Acad Sci U S A. 1999 Feb 2;96(3):903-8. PMID:[http:// | Alpha-helix nucleation by a calcium-binding peptide loop., Siedlecka M, Goch G, Ejchart A, Sticht H, Bierzyski A, Proc Natl Acad Sci U S A. 1999 Feb 2;96(3):903-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9927666 9927666] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: nmr structure]] | [[Category: nmr structure]] | ||
''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 12:58:04 2008'' | ||
Revision as of 13:58, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CALCIUM-BINDING PEPTIDE, NMR, 30 STRUCTURES
OverviewOverview
A 12-residue peptide AcDKDGDGYISAAENH2 analogous to the third calcium-binding loop of calmodulin strongly coordinates lanthanide ions (K = 10(5) M-1). When metal saturated, the peptide adopts a very rigid structure, the same as in the native protein, with three last residues AAE fixed in the alpha-helical conformation. Therefore, the peptide provides an ideal helix nucleation site for peptide segments attached to its C terminus. NMR and CD investigations of peptide AcDKDGDGYISAAEAAAQNH2 presented in this paper show that residues A13-Q16 form an alpha-helix of very high stability when the La3+ ion is bound to the D1-E12 loop. In fact, the lowest estimates of the helix content in this segment give values of at least 80% at 1 degreesC and 70% at 25 degreesC. This finding is not compatible with existing helix-coil transition theories and helix propagation parameters, s, reported in the literature. We conclude, therefore, that the initial steps of helix propagation are characterized by much larger s values, whereas helix nucleation is even more unfavorable than is believed. In light of our findings, thermodynamics of the nascent alpha-helices is discussed. The problem of CD spectra of very short alpha-helices is also addressed.
DiseaseDisease
Known diseases associated with this structure: Cavernous malformations of CNS and retina OMIM:[604214], Cerebral cavernous malformations-1 OMIM:[604214], Hyperkeratotic cutaneous capillary-venous malformations associated with cerebral capillary malformations OMIM:[604214], Leukemia, acute T-cell lymphoblastic OMIM:[603025], Leukemia, acute myeloid OMIM:[603025]
About this StructureAbout this Structure
1NKF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Alpha-helix nucleation by a calcium-binding peptide loop., Siedlecka M, Goch G, Ejchart A, Sticht H, Bierzyski A, Proc Natl Acad Sci U S A. 1999 Feb 2;96(3):903-8. PMID:9927666
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