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1nkf

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Revision as of 10:58, 20 March 2008 by OCA (Talk | contribs)
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PDB ID 1nkf

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Ligands: , and
Coordinates: save as pdb, mmCIF, xml



CALCIUM-BINDING PEPTIDE, NMR, 30 STRUCTURES


Contents

Overview

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.

Disease

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 Structure

1NKF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

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:9927666

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