1bfa

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1bfa.gif|left|200px]]<br /><applet load="1bfa" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1bfa.gif|left|200px]]
-
caption="1bfa, resolution 2.20&Aring;" />
+
 
-
'''RECOMBINANT BIFUNCTIONAL HAGEMAN FACTOR/AMYLASE INHIBITOR FROM MAIZE'''<br />
+
{{Structure
 +
|PDB= 1bfa |SIZE=350|CAPTION= <scene name='initialview01'>1bfa</scene>, resolution 2.20&Aring;
 +
|SITE= <scene name='pdbsite=SLE:Cleaved+By+Target+SER+Proteases'>SLE</scene>
 +
|LIGAND=
 +
|ACTIVITY=
 +
|GENE= 7N-CHFI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4577 Zea mays])
 +
}}
 +
 
 +
'''RECOMBINANT BIFUNCTIONAL HAGEMAN FACTOR/AMYLASE INHIBITOR FROM MAIZE'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1BFA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. Known structural/functional Site: <scene name='pdbsite=SLE:Cleaved+By+Target+SER+Proteases'>SLE</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BFA OCA].
+
1BFA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BFA OCA].
==Reference==
==Reference==
-
Structural determinants of the bifunctional corn Hageman factor inhibitor: x-ray crystal structure at 1.95 A resolution., Behnke CA, Yee VC, Trong IL, Pedersen LC, Stenkamp RE, Kim SS, Reeck GR, Teller DC, Biochemistry. 1998 Nov 3;37(44):15277-88. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9799488 9799488]
+
Structural determinants of the bifunctional corn Hageman factor inhibitor: x-ray crystal structure at 1.95 A resolution., Behnke CA, Yee VC, Trong IL, Pedersen LC, Stenkamp RE, Kim SS, Reeck GR, Teller DC, Biochemistry. 1998 Nov 3;37(44):15277-88. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9799488 9799488]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Zea mays]]
[[Category: Zea mays]]
Line 24: Line 33:
[[Category: serine protease inhibitor]]
[[Category: serine protease inhibitor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:39 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:10:14 2008''

Revision as of 08:10, 20 March 2008


PDB ID 1bfa

Drag the structure with the mouse to rotate
, resolution 2.20Å
Sites:
Gene: 7N-CHFI (Zea mays)
Coordinates: save as pdb, mmCIF, xml



RECOMBINANT BIFUNCTIONAL HAGEMAN FACTOR/AMYLASE INHIBITOR FROM MAIZE


Overview

Corn Hageman factor inhibitor (CHFI) is a bifunctional 127 residue, 13.6 kDa protein isolated from corn seeds. It inhibits mammalian trypsin and Factor XIIa (Hageman Factor) of the contact pathway of coagulation as well as alpha-amylases from several insect species. Among the plasma proteinases, CHFI specifically inhibits Factor XIIa without affecting the activity of other coagulation proteinases. We have isolated CHFI from corn and determined the crystallographic structure at 1.95 A resolution. Additionally, we have solved the structure of the recombinant protein produced in Escherichia coli at 2.2 A resolution. The two proteins are essentially identical. The proteinase binding loop is in the canonical conformation for proteinase inhibitors. In an effort to understand alpha-amylase inhibition by members of the family of 25 cereal trypsin/alpha-amylase inhibitors, we have made three-dimensional models of several proteins in the family based on the CHFI coordinates and the coordinates determined for wheat alpha-amylase inhibitor 0.19 [Oda, Y., Matsunaga, T., Fukuyama, K., Miyazaki, T., and Morimoto, T. (1997) Biochemistry 36, 13503-13511]. From an analysis of the models and a structure-based sequence analysis, we propose a testable hypothesis for the regions of these proteins which bind alpha-amylase. In the course of the investigations, we have found that the cereal trypsin/alpha-amylase inhibitor family is evolutionarily related to the family of nonspecific lipid-transfer proteins of plants. This is a new addition to the group which now consists of the trypsin/alpha-amylase inhibitors, 2S seed storage albumins, and the lipid-transfer family. Apparently, the four-helix conformation has been a successful vehicle in plant evolution for providing protection from predators, food for the embryo, and lipid transfer.

About this Structure

1BFA is a Single protein structure of sequence from Zea mays. Full crystallographic information is available from OCA.

Reference

Structural determinants of the bifunctional corn Hageman factor inhibitor: x-ray crystal structure at 1.95 A resolution., Behnke CA, Yee VC, Trong IL, Pedersen LC, Stenkamp RE, Kim SS, Reeck GR, Teller DC, Biochemistry. 1998 Nov 3;37(44):15277-88. PMID:9799488

Page seeded by OCA on Thu Mar 20 10:10:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools