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.


1e8a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1e8a.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1e8a.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1e8a| PDB=1e8a | SCENE= }}
{{STRUCTURE_1e8a| PDB=1e8a | SCENE= }}
-
'''THE THREE-DIMENSIONAL STRUCTURE OF HUMAN S100A12'''
+
===THE THREE-DIMENSIONAL STRUCTURE OF HUMAN S100A12===
-
==Overview==
+
<!--
-
The crystal structure of human EF-hand calcium-binding protein S100A12 in its calcium-bound form has been determined to 1.95 A resolution by molecular replacement using the structure of the S100B protein. The S100 family members are homologous to calmodulin and other related EF-hand calcium-binding proteins. Like the majority of S100 proteins, S100A12 is a dimer, with the interface between the two subunits being composed mostly of hydrophobic residues. The fold of S100A12 is similar to the other known crystal and solution structures of S100 proteins, except for the linker region between the two EF-hand motifs. Sequence and structure comparison between members of the S100 family suggests that the target-binding region in S100A12 is formed by the linker region and C-terminal residues of one subunit and the N-terminal residues of another subunit of the dimer. The N-terminal region of the target-binding site includes two glutamates that are conserved in most of the S100 sequences. The comparison also provided a better understanding of the role of the residues important for intra- and inter-subunit hydrophobic interactions. The precise role of S100A12 in cell behaviour is yet undefined, as is the case for the whole family, although it has been shown that the interaction of S100A12 with the RAGE receptor is implicated in inflammatory response.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11134923}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11134923 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11134923}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: S100 protein]]
[[Category: S100 protein]]
[[Category: X-ray structure]]
[[Category: X-ray structure]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:47:13 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:18:33 2008''

Revision as of 21:18, 30 June 2008

Image:1e8a.png

Template:STRUCTURE 1e8a

THE THREE-DIMENSIONAL STRUCTURE OF HUMAN S100A12

Template:ABSTRACT PUBMED 11134923

About this Structure

1E8A is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The three-dimensional structure of human S100A12., Moroz OV, Antson AA, Murshudov GN, Maitland NJ, Dodson GG, Wilson KS, Skibshoj I, Lukanidin EM, Bronstein IB, Acta Crystallogr D Biol Crystallogr. 2001 Jan;57(Pt 1):20-9. PMID:11134923

Page seeded by OCA on Tue Jul 1 00:18:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e8a"
Personal tools