This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1hmf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hmf.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1hmf.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hmf| PDB=1hmf | SCENE= }}
{{STRUCTURE_1hmf| PDB=1hmf | SCENE= }}
-
'''STRUCTURE OF THE HMG BOX MOTIF IN THE B-DOMAIN OF HMG1'''
+
===STRUCTURE OF THE HMG BOX MOTIF IN THE B-DOMAIN OF HMG1===
-
==Overview==
+
<!--
-
The conserved, abundant chromosomal protein HMG1 consists of two highly homologous, folded, basic DNA-binding domains, each of approximately 80 amino acid residues, and an acidic C-terminal tail. Each folded domain represents an 'HMG box', a sequence motif recently recognized in certain sequence-specific DNA-binding proteins and which also occurs in abundant HMG1-like proteins that bind to DNA without sequence specificity. The HMG box is defined by a set of highly conserved residues (most distinctively aromatic and basic) and appears to define a novel DNA-binding structural motif. We have expressed the HMG box region of the B-domain of rat HMG1 (residues 88-164 of the intact protein) in Escherichia coli and we describe here the determination of its structure by 2D 1H-NMR spectroscopy. There are three alpha-helices (residues 13-29, 34-48 and 50-74), which together account for approximately 75% of the total residues and contain many of the conserved basic and aromatic residues. Strikingly, the molecule is L-shaped, the angle of approximately 80 degrees between the two arms being defined by a cluster of conserved, predominantly aromatic, residues. The distinctive shape of the HMG box motif, which is distinct from hitherto characterized DNA-binding motifs, may be significant in relation to its recognition of four-way DNA junctions.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8467791}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8467791 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8467791}}
==About this Structure==
==About this Structure==
-
1HMF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HMF OCA].
+
1HMF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HMF OCA].
==Reference==
==Reference==
Line 29: Line 33:
[[Category: Weir, H M.]]
[[Category: Weir, H M.]]
[[Category: Dna-binding]]
[[Category: Dna-binding]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:00:55 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:23:59 2008''

Revision as of 05:24, 1 July 2008

Image:1hmf.png

Template:STRUCTURE 1hmf

STRUCTURE OF THE HMG BOX MOTIF IN THE B-DOMAIN OF HMG1

Template:ABSTRACT PUBMED 8467791

About this Structure

1HMF is a Single protein structure of sequence from Rattus norvegicus. Full experimental information is available from OCA.

Reference

Structure of the HMG box motif in the B-domain of HMG1., Weir HM, Kraulis PJ, Hill CS, Raine AR, Laue ED, Thomas JO, EMBO J. 1993 Apr;12(4):1311-9. PMID:8467791

Page seeded by OCA on Tue Jul 1 08:23:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hmf"
Personal tools