1tye: Difference between revisions

Revision as of 04:29, 29 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:1tye.png

Template:STRUCTURE 1tye

Structural basis for allostery in integrins and binding of ligand-mimetic therapeutics to the platelet receptor for fibrinogenStructural basis for allostery in integrins and binding of ligand-mimetic therapeutics to the platelet receptor for fibrinogen

Template:ABSTRACT PUBMED 15378069

About this StructureAbout this Structure

1TYE is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics., Xiao T, Takagi J, Coller BS, Wang JH, Springer TA, Nature. 2004 Nov 4;432(7013):59-67. Epub 2004 Sep 19. PMID:15378069

Page seeded by OCA on Tue Jul 29 04:29:34 2008

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

OCA

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-'''Structural basis for allostery in integrins and binding of ligand-mimetic therapeutics to the platelet receptor for fibrinogen'''
+===Structural basis for allostery in integrins and binding of ligand-mimetic therapeutics to the platelet receptor for fibrinogen===
-==Overview==
+<!--
-Integrins are important adhesion receptors in all Metazoa that transmit conformational change bidirectionally across the membrane. Integrin alpha and beta subunits form a head and two long legs in the ectodomain and span the membrane. Here, we define with crystal structures the atomic basis for allosteric regulation of the conformation and affinity for ligand of the integrin ectodomain, and how fibrinogen-mimetic therapeutics bind to platelet integrin alpha(IIb)beta3. Allostery in the beta3 I domain alters three metal binding sites, associated loops and alpha1- and alpha7-helices. Piston-like displacement of the alpha7-helix causes a 62 degrees reorientation between the beta3 I and hybrid domains. Transmission through the rigidly connected plexin/semaphorin/integrin (PSI) domain in the upper beta3 leg causes a 70 A separation between the knees of the alpha and beta legs. Allostery in the head thus disrupts interaction between the legs in a previously described low-affinity bent integrin conformation, and leg extension positions the high-affinity head far above the cell surface.
+The line below this paragraph, {{ABSTRACT_PUBMED_15378069}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Platelet integrin alphaiibbeta3]]
 [[Category: Therapeutic antagonism]]
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