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1g91
From Proteopedia
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[[Image:1g91.jpg|left|200px]] | [[Image:1g91.jpg|left|200px]] | ||
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'''SOLUTION STRUCTURE OF MYELOID PROGENITOR INHIBITORY FACTOR-1 (MPIF-1)''' | '''SOLUTION STRUCTURE OF MYELOID PROGENITOR INHIBITORY FACTOR-1 (MPIF-1)''' | ||
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[[Category: Rajarathnam, K.]] | [[Category: Rajarathnam, K.]] | ||
[[Category: Rohrer, T.]] | [[Category: Rohrer, T.]] | ||
| - | [[Category: | + | [[Category: Ccl23]] |
| - | [[Category: | + | [[Category: Chemokine]] |
| - | [[Category: | + | [[Category: Ckb8]] |
| - | [[Category: | + | [[Category: Cytokine]] |
| - | [[Category: | + | [[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 | + | |
Revision as of 14:17, 2 May 2008
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
Categories: Homo sapiens | Single protein | Gentz, R. | Li, Y. | Rajarathnam, K. | Rohrer, T. | Ccl23 | Chemokine | Ckb8 | Cytokine | Mpif-1
