1ghc: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:1ghc.jpg|left|200px]]
[[Image:1ghc.jpg|left|200px]]


{{Structure
<!--
|PDB= 1ghc |SIZE=350|CAPTION= <scene name='initialview01'>1ghc</scene>
The line below this paragraph, containing "STRUCTURE_1ghc", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND=
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY=  
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_1ghc| PDB=1ghc  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ghc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghc OCA], [http://www.ebi.ac.uk/pdbsum/1ghc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ghc RCSB]</span>
}}


'''HOMO-AND HETERONUCLEAR TWO-DIMENSIONAL NMR STUDIES OF THE GLOBULAR DOMAIN OF HISTONE H1: FULL ASSIGNMENT, TERTIARY STRUCTURE, AND COMPARISON WITH THE GLOBULAR DOMAIN OF HISTONE H5'''
'''HOMO-AND HETERONUCLEAR TWO-DIMENSIONAL NMR STUDIES OF THE GLOBULAR DOMAIN OF HISTONE H1: FULL ASSIGNMENT, TERTIARY STRUCTURE, AND COMPARISON WITH THE GLOBULAR DOMAIN OF HISTONE H5'''
Line 33: Line 30:
[[Category: Wodak, S J.]]
[[Category: Wodak, S J.]]
[[Category: Wyns, L.]]
[[Category: Wyns, L.]]
[[Category: chromosomal protein]]
[[Category: Chromosomal protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:33:38 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:44:02 2008''

Revision as of 17:33, 2 May 2008

File:1ghc.jpg

Template:STRUCTURE 1ghc

HOMO-AND HETERONUCLEAR TWO-DIMENSIONAL NMR STUDIES OF THE GLOBULAR DOMAIN OF HISTONE H1: FULL ASSIGNMENT, TERTIARY STRUCTURE, AND COMPARISON WITH THE GLOBULAR DOMAIN OF HISTONE H5


OverviewOverview

The globular domain of chicken histone H1 (GH1) has been studied by 1H homonuclear and 1H-15N heteronuclear 2D NMR spectroscopy. After the full assignment of the proton and 15N resonances, the tertiary structure of GH1 was determined by an iterative procedure using distance geometry and restrained simulated annealing. The secondary structure elements of GH1, three helices (S5-A16, S24-A34, N42-K56) followed by a beta-hairpin (L59-L73), are folded in a manner very similar to the corresponding parts of the globular domain of chicken histone H5 (GH5) [Clore et al. (1987) EMBO J. 6, 1833-1842; Ramakrishnan et al. (1993) Nature 362, 219-223]. However, subtle differences are detected between the two structures and between the electrostatic potentials surrounding the molecules. The most important differences are located in the loop between the second and third helices, a region that could be responsible for the different affinity for DNA. The most positively charged regions are not found in exactly the same position in GH1 and GH5. Nevertheless, their location seems to agree with the model where nucleosome binding takes place through contact points located at one DNA terminus and close to the dyad axis of the nucleosome [Schwabe & Travers (1993) Curr. Biol. 3, 628-630].

About this StructureAbout this Structure

1GHC is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

ReferenceReference

Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: full assignment, tertiary structure, and comparison with the globular domain of histone H5., Cerf C, Lippens G, Ramakrishnan V, Muyldermans S, Segers A, Wyns L, Wodak SJ, Hallenga K, Biochemistry. 1994 Sep 20;33(37):11079-86. PMID:7727360 Page seeded by OCA on Fri May 2 17:33:38 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA