2b3l: Difference between revisions

Revision as of 15:11, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2b3l.png

Template:STRUCTURE 2b3l

Crystal structure of type I human methionine aminopeptidase in the apo formCrystal structure of type I human methionine aminopeptidase in the apo form

Template:ABSTRACT PUBMED 16274222

About this StructureAbout this Structure

2B3L is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for the functional differences between type I and type II human methionine aminopeptidases., Addlagatta A, Hu X, Liu JO, Matthews BW, Biochemistry. 2005 Nov 15;44(45):14741-9. PMID:16274222

Page seeded by OCA on Sun Jul 27 15:11:17 2008

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OCA

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-'''Crystal structure of type I human methionine aminopeptidase in the apo form'''
+===Crystal structure of type I human methionine aminopeptidase in the apo form===
-==Overview==
+<!--
-Determination of the crystal structure of human MetAP1 makes it possible, for the first time, to compare the structures of a Type I and a Type II methionine aminopeptidase (MetAP) from the same organism. Comparison of the Type I enzyme with the previously reported complex of ovalicin with Type II MetAP shows that the active site of the former is reduced in size and would incur steric clashes with the bound inhibitor. This explains why ovalicin and related anti-angiogenesis inhibitors target Type II human MetAP but not Type I. The differences in both size and shape of the active sites between MetAP1 and MetAP2 also help to explain their different substrate specificity. In the presence of excess Co(2+), a third cobalt ion binds in the active site region, explaining why metal ions in excess can be inhibitory. Also, the N-terminal region of the protein contains three distinct Pro-x-x-Pro motifs, supporting the prior suggestion that this region of the protein may participate in binding to the ribosome.
+The line below this paragraph, {{ABSTRACT_PUBMED_16274222}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16274222 is the PubMed ID number.
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 ==About this Structure==
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 [[Category: Methionine aminopeptidase]]
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