1hoe: Difference between revisions

Revision as of 14:03, 21 February 2008

CRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467A

OverviewOverview

The crystal and molecular structure of the alpha-amylase inhibitor Hoe-467A has been determined and refined at high resolution. The polypeptide chain is folded in two triple-stranded sheets, which form a barrel. The topology of folding is as found in the immunoglobulin domains. The amino acid triplet Trp18-Arg19-Tyr20 has an exceptional conformation and position in the molecule and is possibly involved in inhibitory activity.

About this StructureAbout this Structure

1HOE is a Single protein structure of sequence from Streptomyces tendae. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor Hoe-467A., Pflugrath JW, Wiegand G, Huber R, Vertesy L, J Mol Biol. 1986 May 20;189(2):383-6. PMID:3489104

Page seeded by OCA on Thu Feb 21 13:03:32 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1hoe.gif|left|200px]]<br /><applet load="1hoe" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1hoe.gif|left|200px]]<br /><applet load="1hoe" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1hoe, resolution 2.0&Aring;" />
 '''CRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467A'''<br />
 ==Overview==
-The crystal and molecular structure of the alpha-amylase inhibitor, Hoe-467A has been determined and refined at high resolution. The, polypeptide chain is folded in two triple-stranded sheets, which form a, barrel. The topology of folding is as found in the immunoglobulin domains., The amino acid triplet Trp18-Arg19-Tyr20 has an exceptional conformation, and position in the molecule and is possibly involved in inhibitory, activity.
+The crystal and molecular structure of the alpha-amylase inhibitor Hoe-467A has been determined and refined at high resolution. The polypeptide chain is folded in two triple-stranded sheets, which form a barrel. The topology of folding is as found in the immunoglobulin domains. The amino acid triplet Trp18-Arg19-Tyr20 has an exceptional conformation and position in the molecule and is possibly involved in inhibitory activity.
 ==About this Structure==
-HOE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_tendae Streptomyces tendae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HOE OCA].
+HOE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_tendae Streptomyces tendae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HOE OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Streptomyces tendae]]
 [[Category: Huber, R.]]
-[[Category: Pflugrath, J.W.]]
+[[Category: Pflugrath, J W.]]
 [[Category: Wiegand, G.]]
 [[Category: glycosidase inhibitor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:42:38 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:32 2008''