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| - | [[Image:1ty5.gif|left|200px]] | + | #REDIRECT [[2vdm]] This PDB entry is obsolete and replaced by 2vdm |
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| - | {{Structure
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| - | |PDB= 1ty5 |SIZE=350|CAPTION= <scene name='initialview01'>1ty5</scene>, resolution 2.90Å
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| - | |SITE=
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| - | |LIGAND= <scene name='pdbligand=AGG:TIROFIBAN'>AGG</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>
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| - | |ACTIVITY=
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| - | |GENE= ITGAB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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| - | |DOMAIN=
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| - | |RELATEDENTRY=[[1txv|1TXV]], [[1ty3|1TY3]], [[1ty6|1TY6]], [[1ty7|1TY7]], [[1tye|1TYE]]
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| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ty5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ty5 OCA], [http://www.ebi.ac.uk/pdbsum/1ty5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ty5 RCSB]</span>
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| - | }}
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| - | '''Structural basis for allostery in integrins and binding of ligand-mimetic therapeutics to the platelet receptor for fibrinogen'''
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| - | ==Overview==
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| - | 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.
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| - | ==About this Structure==
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| - | 1TY5 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TY5 OCA].
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| - | ==Reference==
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| - | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15378069 15378069]
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| - | [[Category: Homo sapiens]]
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| - | [[Category: Mus musculus]]
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| - | [[Category: Protein complex]]
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| - | [[Category: Coller, B S.]]
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| - | [[Category: Springer, T A.]]
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| - | [[Category: Takagi, J.]]
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| - | [[Category: Wang, J H.]]
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| - | [[Category: Xiao, T.]]
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| - | [[Category: allostery]]
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| - | [[Category: crystal structure]]
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| - | [[Category: fibrinogen binding]]
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| - | [[Category: platelet integrin alphaiibbeta3]]
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| - | [[Category: therapeutic antagonism]]
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:02:43 2008''
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