1ghc: Difference between revisions

Revision as of 05:17, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ghc.png

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 H5HOMO-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

Template:ABSTRACT PUBMED 7727360

About this StructureAbout this Structure

1GHC is a Single protein structure of sequence from Gallus gallus. Full experimental 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 Tue Jul 1 05:17:13 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1ghc.jpg|left|200px]]
+{{Seed}}
+[[Image:1ghc.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1ghc|  PDB=1ghc  |  SCENE=  }}
-'''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===
-==Overview==
+<!--
-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 &amp; Travers (1993) Curr. Biol. 3, 628-630].
+The line below this paragraph, {{ABSTRACT_PUBMED_7727360}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7727360 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7727360}}
 ==About this Structure==
-GHC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHC OCA].
+GHC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHC OCA].
 ==Reference==
@@ Line 31: / Line 35: @@
 [[Category: Wyns, L.]]
 [[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 Tue Jul  1 05:17:13 2008''