1fy3
From Proteopedia
(New page: 200px<br /> <applet load="1fy3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fy3, resolution 1.89Å" /> '''[G175Q]HBP, A MUTAN...) |
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| - | [[Image:1fy3. | + | [[Image:1fy3.jpg|left|200px]]<br /><applet load="1fy3" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1fy3, resolution 1.89Å" /> | caption="1fy3, resolution 1.89Å" /> | ||
'''[G175Q]HBP, A MUTANT OF HUMAN HEPARIN BINDING PROTEIN (CAP37)'''<br /> | '''[G175Q]HBP, A MUTANT OF HUMAN HEPARIN BINDING PROTEIN (CAP37)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FY3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG, CL and EOH as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1FY3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=EOH:'>EOH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FY3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: serine protease homolog]] | [[Category: serine protease homolog]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:49:46 2008'' |
Revision as of 13:49, 15 February 2008
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[G175Q]HBP, A MUTANT OF HUMAN HEPARIN BINDING PROTEIN (CAP37)
Overview
Heparin binding protein (HBP) is an inactive serine protease homologue, with important implications in host defense during infections and, inflammations. Two mutants of human HBP, [R23S,F25E]HBP and [G175Q]HBP, have been produced to investigate structure-function relationships of, residues in the putative lipid A/lipopolysaccharide (LPS) binding site and, BPTI (bovine pancreatic trypsin inhibitor) binding site. The X-ray, structures have been determined at 1.9 A resolution for [G175Q]HBP and at, 2.5 A resolution for the [R23S,F25E]HBP mutant, and the structures have, been fully refined to R-factors of 18.2 % and 20.7 %, respectively. The, G175Q mutation does not alter the overall structure of the protein, but, the ability to bind BPTI has been eliminated, and the mutant mediates only, a limited stimulation of the LPS-induced cytokine release from human, monocytes. The lipid A/LPS binding property of [G175Q]HBP is comparable, with that of native HBP. The R23S,F25E mutations do not affect the binding, of lipid A/LPS and BPTI or the LPS-induced cytokine release from human, monocytes. This shows that two diverse ligands, lipid A/LPS and BPTI, do, not share binding sites. Previously, there was convincing evidence for the, proposed lipid A/LPS binding site of HBP. Unexpectedly, the extensive, structural changes introduced by mutation of Arg23 and Phe25 do not affect, the binding of lipid A/LPS, indicating that another not yet identified, site on HBP is involved in the binding of lipid A/LPS.
About this Structure
1FY3 is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
Reference
Two mutants of human heparin binding protein (CAP37): toward the understanding of the nature of lipid A/LPS and BPTI binding., Kastrup JS, Linde V, Pedersen AK, Stoffer B, Iversen LF, Larsen IK, Rasmussen PB, Flodgaard HJ, Bjorn SE, Proteins. 2001 Mar 1;42(4):442-51. PMID:11170199
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