Integrin beta-3 (P05106)

Basic protein information
UniProt Gene ITGB3
Organism Homo sapiens
Keywords 3D-structure, Alternative splicing, Cell adhesion, Cell junction, Cell membrane, Cell projection, Direct protein sequencing, Disease mutation, Disulfide bond, Glycoprotein, Host cell receptor for virus entry, Host-virus interaction, Integrin, Membrane, Phosphoprotein, Polymorphism, Postsynaptic cell membrane, Receptor, Reference proteome, Repeat, Signal, Synapse, Transmembrane, Transmembrane helix
MemMoRF data
Warning: residue numbering from UniProt, PDB, and papers may differ.
MemMoRF ID Region Supporting statements
9228 770-784
Category: MemMoRF
Type: disorder to order
Localization: intracellular
IDR Proof: DisProt, DIBS, calculations
MemInteract Proof: calculations, papers
"As expected, TMproxH was predicted to partition into the bilayer perpendicular to the membrane as an extension of the TM helix, whereas CytoH1 and CytoH2 were predicted to lie along the membrane surface, stabilized by hydrophobic residues Phe727 and Phe730 in CytoH1 and Leu746, Tyr747, Ala750, Phe754, and Ile757 in CytoH2" ... "HDX of the β3 cytoplasmic domain conjugated to lipid." ... "Asn743-Thr762 was not observed in the absence the bilayers [fig4]" ... Results of HDX experiments (Admin): "the intermediate fragment spanning a portion of the loop and all of CytoH2 had four protected amides (Asn743-Thr762); and the most C-terminal fragment (Asn756-Thr762) had only one protected amide. These results confirmed the location of the helices identified by NMR, as well as the hierarchy of increasing disorder that progresses from the N terminus to the C terminus of the β3 cytoplasmic domain." (PMID:21156831)
"At the TM-CT border, the spatial positions of the positively charged groups of αIIb K989/β3 K716 (Fig. 1D) suggest that they begin the cytoplasmic regions. However, it is possible that the side chains following membrane-proximal residues αIIb V990-F993, β3 L717-I721 are inserted into or anchored onto the membrane (Fig. 1D), which may stabilize the relative orientations of the TM helices." (PMID:19805198)
"Moreover, we have demonstrated that several residues of β3NP (Trp739, Thr741, Ala742, Pro745, and Tyr747) could interact with DPC micelles and these interactions initiate the formation of a second short α-helical region (Leu746-Asn756), which is not generally observed in either aqueous β3 or αIIbβ3 heterodimer" ... ". In this study, we also have accumulated the first direct evidence that tyrosine phosphorylation affects the structure and the association of 3CT with membrane." (PMID:21956114)
"Immediately next to the loop is the N744PLY747 motif that forms an inverse turn, which is the start point for the second helix" ... "The formation of the C-terminal helix is surprising, because it was absent in the structure of the αIIb/β3 tail complex in aqueous solution. Because no long-range NOEs were observed between the N- and C-terminal helices, the formation of the C-terminal helix is likely induced and stabilized by the docking of the NPLY turn onto DPC." (PMID:15024114)
9227 751-766
Category: MemMoRF
Type: disorder to order
Localization: intracellular
IDR Proof: DisProt, DIBS
MemInteract Proof: calculations, papers

"Moreover, we have demonstrated that several residues of β3NP (Trp739, Thr741, Ala742, Pro745, and Tyr747) could interact with DPC micelles and these interactions initiate the formation of a second short α-helical region (Leu746-Asn756), which is not generally observed in either aqueous β3 or αIIbβ3 heterodimer" ... ". In this study, we also have accumulated the first direct evidence that tyrosine phosphorylation affects the structure and the association of 3CT with membrane." (PMID:21956114)
"As expected, TMproxH was predicted to partition into the bilayer perpendicular to the membrane as an extension of the TM helix, whereas CytoH1 and CytoH2 were predicted to lie along the membrane surface, stabilized by hydrophobic residues Phe727 and Phe730 in CytoH1 and Leu746, Tyr747, Ala750, Phe754, and Ile757 in CytoH2" ... "HDX of the β3 cytoplasmic domain conjugated to lipid." ... "Asn743-Thr762 was not observed in the absence the bilayers [fig4]" (PMID:21156831)
View on BMRB
Strutures
View on PDBe
Disease/MIM
MIM gene: 173470
phenotype: Bleeding disorder, platelet-type 16 (BDPLT16) 187800
phenotype: Glanzmann thrombasthenia (GT) 273800
Genetic variations/dbSNP
a.a. change Type dbSNP ID Disesase name
p.Ser778Pro Disease within MemMoRF region 121918447 Glanzmann
p.Leu59Pro Polymorphism 5918 -
p.Cys64Tyr Disease 74554539 Glanzmann
p.Leu66Arg Polymorphism 36080296 -
p.Arg119Trp Disease 781062792 Glanzmann
p.Tyr141Cys Disease - Glanzmann
p.Leu143Trp Disease 121918452 Glanzmann
p.Met144Arg Disease 77963874 Glanzmann
p.Asp145Tyr Disease 121918445 Glanzmann
p.Asp145Asn Disease - Glanzmann
p.Met150Val Disease 767548512 Glanzmann
p.Thr166Ile Polymorphism 74708909 -
p.Arg169Gln Polymorphism 5917 -
p.Ser188Leu Disease 143146734 Glanzmann
p.Leu222Pro Disease 79208797 Glanzmann
p.Arg240Gln Disease 121918444 Glanzmann
p.Arg240Trp Disease 121918446 Glanzmann
p.Arg242Gln Disease 377162158 Glanzmann
p.Asp243Val Disease - Glanzmann
p.Gly247Asp Disease 79560904 Glanzmann
p.Lys279Met Disease 79775494 Glanzmann
p.Leu288Pro Disease - Glanzmann
p.His306Pro Disease 13306476 Glanzmann
p.Met321Leu Disease - Glanzmann
p.Ile330Asn Disease - Glanzmann
p.Cys400Tyr Disease 121918449 Glanzmann
p.Pro433Ala Polymorphism 121918448 -
p.Val453Ile Polymorphism 5921 -
p.Arg515Gln Polymorphism 13306487 -
p.Cys532Tyr Disease - Glanzmann
p.Cys568Arg Disease - Glanzmann
p.Cys586Phe Disease - Glanzmann
p.Cys586Arg Disease - Glanzmann
p.Gly598Ser Disease - Glanzmann
p.Cys601Arg Disease 747534508 Glanzmann
p.Gly605Ser Disease 144884023 Glanzmann
p.Arg662Cys Polymorphism 151219882 -
p.Asp749His Disease 398122372 Bleeding
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https://string-db.org/cgi/network?identifiers=/P05106
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