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.


2ozo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==Overview==
==Overview==
-
ZAP-70, a cytoplasmic tyrosine kinase required for T cell antigen receptor, signaling, is controlled by a regulatory segment that includes a tandem, SH2 unit responsible for binding to immunoreceptor tyrosine-based, activation motifs (ITAMs). The crystal structure of autoinhibited ZAP-70, reveals that the inactive kinase domain adopts a conformation similar to, that of cyclin-dependent kinases and Src kinases. The autoinhibitory, mechanism of ZAP-70 is, however, distinct and involves interactions, between the regulatory segment and the hinge region of the kinase domain, that reduce its flexibility. Two tyrosine residues in the SH2-kinase, linker that activate ZAP-70 when phosphorylated are involved in, aromatic-aromatic interactions that connect the linker to the kinase, domain. These interactions are inconsistent with ITAM binding, suggesting, that destabilization of this autoinhibited ZAP-70 conformation is the, first step in kinase activation.
+
ZAP-70, a cytoplasmic tyrosine kinase required for T cell antigen receptor signaling, is controlled by a regulatory segment that includes a tandem SH2 unit responsible for binding to immunoreceptor tyrosine-based activation motifs (ITAMs). The crystal structure of autoinhibited ZAP-70 reveals that the inactive kinase domain adopts a conformation similar to that of cyclin-dependent kinases and Src kinases. The autoinhibitory mechanism of ZAP-70 is, however, distinct and involves interactions between the regulatory segment and the hinge region of the kinase domain that reduce its flexibility. Two tyrosine residues in the SH2-kinase linker that activate ZAP-70 when phosphorylated are involved in aromatic-aromatic interactions that connect the linker to the kinase domain. These interactions are inconsistent with ITAM binding, suggesting that destabilization of this autoinhibited ZAP-70 conformation is the first step in kinase activation.
 +
 
 +
==Disease==
 +
Known diseases associated with this structure: Selective T-cell defect OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176947 176947]]
==About this Structure==
==About this Structure==
Line 17: Line 20:
[[Category: Cao, X.]]
[[Category: Cao, X.]]
[[Category: Deindl, S.]]
[[Category: Deindl, S.]]
-
[[Category: Kadlecek, T.A.]]
+
[[Category: Kadlecek, T A.]]
[[Category: Kuriyan, J.]]
[[Category: Kuriyan, J.]]
[[Category: Weiss, A.]]
[[Category: Weiss, A.]]
Line 29: Line 32:
[[Category: tcr signaling]]
[[Category: tcr signaling]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:59:18 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:24:16 2008''

Revision as of 16:24, 21 February 2008


2ozo, resolution 2.600Å

Drag the structure with the mouse to rotate

Autoinhibited intact human ZAP-70

Contents

Overview

ZAP-70, a cytoplasmic tyrosine kinase required for T cell antigen receptor signaling, is controlled by a regulatory segment that includes a tandem SH2 unit responsible for binding to immunoreceptor tyrosine-based activation motifs (ITAMs). The crystal structure of autoinhibited ZAP-70 reveals that the inactive kinase domain adopts a conformation similar to that of cyclin-dependent kinases and Src kinases. The autoinhibitory mechanism of ZAP-70 is, however, distinct and involves interactions between the regulatory segment and the hinge region of the kinase domain that reduce its flexibility. Two tyrosine residues in the SH2-kinase linker that activate ZAP-70 when phosphorylated are involved in aromatic-aromatic interactions that connect the linker to the kinase domain. These interactions are inconsistent with ITAM binding, suggesting that destabilization of this autoinhibited ZAP-70 conformation is the first step in kinase activation.

Disease

Known diseases associated with this structure: Selective T-cell defect OMIM:[176947]

About this Structure

2OZO is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Non-specific protein-tyrosine kinase, with EC number 2.7.10.2 Full crystallographic information is available from OCA.

Reference

Structural basis for the inhibition of tyrosine kinase activity of ZAP-70., Deindl S, Kadlecek TA, Brdicka T, Cao X, Weiss A, Kuriyan J, Cell. 2007 May 18;129(4):735-46. PMID:17512407

Page seeded by OCA on Thu Feb 21 18:24:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools