1jtz: Difference between revisions

Revision as of 20:51, 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:1jtz.png

Template:STRUCTURE 1jtz

CRYSTAL STRUCTURE OF TRANCE/RANKL CYTOKINE.CRYSTAL STRUCTURE OF TRANCE/RANKL CYTOKINE.

Template:ABSTRACT PUBMED 11581298

About this StructureAbout this Structure

1JTZ is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the TRANCE/RANKL cytokine reveals determinants of receptor-ligand specificity., Lam J, Nelson CA, Ross FP, Teitelbaum SL, Fremont DH, J Clin Invest. 2001 Oct;108(7):971-9. PMID:11581298

Page seeded by OCA on Tue Jul 1 20:51:31 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1jtz.gif|left|200px]]
+{{Seed}}
+[[Image:1jtz.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1jtz|  PDB=1jtz  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF TRANCE/RANKL CYTOKINE.'''
+===CRYSTAL STRUCTURE OF TRANCE/RANKL CYTOKINE.===
-==Overview==
+<!--
-RANK, the receptor activator of NF-kappaB, and its ligand RANKL (initially termed TRANCE, also termed ODF and OPGL), are a TNF superfamily receptor-ligand pair that govern the development and function of osteoclasts, lymphoid tissue, and mammary epithelium. While TNF family cytokines share a common structural scaffold, individual receptor-ligand pairs associate with high specificity. Given the low level of amino acid conservation among members of the TNF superfamily, the means by which these molecules achieve specificity cannot be completely understood without knowledge of their three-dimensional structures. To determine the elements of RANKL that mediate RANK activation, we have crystallized the ectodomain of murine RANKL and solved its structure to a resolution of 2.6 A. RANKL self-associates as a homotrimer with four unique surface loops that distinguish it from other TNF family cytokines. Mutagenesis of selected residues in these loops significantly modulates RANK activation, as evidenced by in vitro osteoclastogenesis, thereby establishing their necessity in mediating the biological activities of RANKL. Such structural determinants of RANKL-RANK specificity may be of relevance in the pharmacologic design of compounds to ameliorate osteopenic disorders of bone.
+The line below this paragraph, {{ABSTRACT_PUBMED_11581298}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11581298 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11581298}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Jellyroll]]
 [[Category: Tumor necrosis factor superfamily member]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:55:08 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 20:51:31 2008''