1gwb
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STRUCTURE OF GLYCOPROTEIN 1B
OverviewOverview
Glycoprotein Ib (GPIb) is a platelet receptor with a critical role in, mediating the arrest of platelets at sites of vascular damage. GPIb binds, to the A1 domain of von Willebrand factor (vWF-A1) at high blood shear, initiating platelet adhesion and contributing to the formation of a, thrombus. To investigate the molecular basis of GPIb regulation and ligand, binding, we have determined the structure of the N-terminal domain of the, GPIb(alpha) chain (residues 1-279). This structure is the first determined, from the cell adhesion/signaling class of leucine-rich repeat (LRR), proteins and reveals the topology of the characteristic disulfide-bonded, flanking regions. The fold consists of an N-terminal beta-hairpin, eight, leucine-rich repeats, a disulfide-bonded loop, and a C-terminal ... [(full description)]
About this StructureAbout this Structure
1GWB is a [Single protein] structure of sequence from [Homo sapiens] with NAG, NDG, PT, SO4 and ACY as [ligands]. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of the platelet glycoprotein Ib(alpha) N-terminal domain reveals an unmasking mechanism for receptor activation., Uff S, Clemetson JM, Harrison T, Clemetson KJ, Emsley J, J Biol Chem. 2002 Sep 20;277(38):35657-63. Epub 2002 Jun 26. PMID:12087105
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- Homo sapiens
- Single protein
- Clemetson, J.
- Clemetson, K.
- Emsley, J.
- Harrison, T.
- Uff, S.
- ACY
- NAG
- NDG
- PT
- SO4
- Bernard soulier syndrome
- Blood coagulation
- Cell adhesion
- Disease mutation
- Glycoprotein
- Glycoprotein 1b
- Hemostasis
- Leucine-rich repeat
- Platelet
- Polymorphism
- Repeat
- Signal
- Transmembrane
- Von willebrand disease