1g91

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1g91.jpg|left|200px]]
[[Image:1g91.jpg|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1g91 |SIZE=350|CAPTION= <scene name='initialview01'>1g91</scene>
+
The line below this paragraph, containing "STRUCTURE_1g91", 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_1g91| PDB=1g91 | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g91 OCA], [http://www.ebi.ac.uk/pdbsum/1g91 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g91 RCSB]</span>
+
-
}}
+
'''SOLUTION STRUCTURE OF MYELOID PROGENITOR INHIBITORY FACTOR-1 (MPIF-1)'''
'''SOLUTION STRUCTURE OF MYELOID PROGENITOR INHIBITORY FACTOR-1 (MPIF-1)'''
Line 29: Line 26:
[[Category: Rajarathnam, K.]]
[[Category: Rajarathnam, K.]]
[[Category: Rohrer, T.]]
[[Category: Rohrer, T.]]
-
[[Category: ccl23]]
+
[[Category: Ccl23]]
-
[[Category: chemokine]]
+
[[Category: Chemokine]]
-
[[Category: ckb8]]
+
[[Category: Ckb8]]
-
[[Category: cytokine]]
+
[[Category: Cytokine]]
-
[[Category: mpif-1]]
+
[[Category: Mpif-1]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:17:44 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:39:14 2008''
+

Revision as of 14:17, 2 May 2008

Template:STRUCTURE 1g91

SOLUTION STRUCTURE OF MYELOID PROGENITOR INHIBITORY FACTOR-1 (MPIF-1)


Overview

MPIF-1, a CC chemokine, is a specific inhibitor of myeloid progenitor cells and is the most potent activator of monocytes. The solution structure of myeloid progenitor inhibitor factor-1 (MPIF-1) has been determined by NMR spectroscopy. The structure reveals that MPIF-1 is a monomer with a well defined core except for termini residues and adopts the chemokine fold of three beta-strands and an overlying alpha-helix. In addition to the four cysteines that characterize most chemokines, MPIF-1 has two additional cysteines that form a disulfide bond. The backbone dynamics indicate that the disulfide bonds and the adjacent residues that include the functionally important N-terminal and N-terminal loop residues show significant dynamics. MPIF-1 is a highly basic protein (pI >9), and the structure reveals distinct positively charged pockets that could be correlated to proteoglycan binding. MPIF-1 is processed from a longer proprotein at the N terminus and the latter is also functional though with reduced potency, and both proteins exist as monomers under a variety of solution conditions. MPIF-1 is therefore unique because longer proproteins of all other chemokines oligomerize in solution. The MPIF-1 structure should serve as a template for future functional studies that could lead to therapeutics for preventing chemotherapy-associated myelotoxicity.

About this Structure

1G91 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Solution structure and dynamics of myeloid progenitor inhibitory factor-1 (MPIF-1), a novel monomeric CC chemokine., Rajarathnam K, Li Y, Rohrer T, Gentz R, J Biol Chem. 2001 Feb 16;276(7):4909-16. Epub 2000 Nov 1. PMID:11060285 Page seeded by OCA on Fri May 2 17:17:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools