This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1z68

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1z68.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1z68.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1z68| PDB=1z68 | SCENE= }}
{{STRUCTURE_1z68| PDB=1z68 | SCENE= }}
-
'''Crystal Structure Of Human Fibroblast Activation Protein alpha'''
+
===Crystal Structure Of Human Fibroblast Activation Protein alpha===
-
==Overview==
+
<!--
-
Fibroblast activation protein alpha (FAPalpha) is highly expressed in epithelial cancers and has been implicated in extracellular matrix remodeling, tumor growth, and metastasis. We present the first high resolution structure for the apoenzyme as well as kinetic data toward small dipeptide substrates. FAPalpha exhibits a dipeptidyl peptidase IV (DPPIV)-like fold, featuring an alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain. Known DPPIV dipeptides are cleaved by FAPalpha with an approximately 100-fold decrease in catalytic efficiency compared with DPPIV. Moreover, FAPalpha, but not DPPIV, possesses endopeptidase activity toward N-terminal benzyloxycarbonyl (Z)-blocked peptides. Comparison of the crystal structures of FAPalpha and DPPIV revealed one major difference in the vicinity of the Glu motif (Glu(203)-Glu(204) for FAPalpha; Glu(205)-Glu(206) for DPPIV) within the active site of the enzyme. Ala(657) in FAPalpha, instead of Asp(663) as in DP-PIV, reduces the acidity in this pocket, and this change could explain the lower affinity for N-terminal amines by FAPalpha. This hypothesis was tested by kinetic analysis of the mutant FAPalpha/A657D, which shows on average an approximately 60-fold increase in the catalytic efficiency, as measured by k(cat)/K(m), for the cleavage of dipeptide substrates. Furthermore, the catalytic efficiency of the mutant is reduced by approximately 350-fold for cleavage of Z-Gly-Pro-7-amino-4-methylcoumarin. Our data provide a clear understanding of the molecular determinants responsible for the substrate specificity and endopeptidase activity of FAPalpha.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15809306}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15809306 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15809306}}
==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Integral membrane serine protease]]
[[Category: Integral membrane serine protease]]
[[Category: Seprase]]
[[Category: Seprase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:13:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:46:30 2008''

Revision as of 12:46, 27 July 2008

Image:1z68.png

Template:STRUCTURE 1z68

Crystal Structure Of Human Fibroblast Activation Protein alpha

Template:ABSTRACT PUBMED 15809306

About this Structure

1Z68 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural and kinetic analysis of the substrate specificity of human fibroblast activation protein alpha., Aertgeerts K, Levin I, Shi L, Snell GP, Jennings A, Prasad GS, Zhang Y, Kraus ML, Salakian S, Sridhar V, Wijnands R, Tennant MG, J Biol Chem. 2005 May 20;280(20):19441-4. Epub 2005 Apr 4. PMID:15809306

Page seeded by OCA on Sun Jul 27 15:46:30 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1z68"
Personal tools