1gwb
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1gwb.gif|left|200px]] | [[Image:1gwb.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1gwb", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | | | + | or leave the SCENE parameter empty for the default display. |
- | | | + | --> |
- | + | {{STRUCTURE_1gwb| PDB=1gwb | SCENE= }} | |
- | + | ||
- | + | ||
- | }} | + | |
'''STRUCTURE OF GLYCOPROTEIN 1B''' | '''STRUCTURE OF GLYCOPROTEIN 1B''' | ||
Line 30: | Line 27: | ||
[[Category: Harrison, T.]] | [[Category: Harrison, T.]] | ||
[[Category: Uff, S.]] | [[Category: Uff, S.]] | ||
- | [[Category: | + | [[Category: Bernard soulier syndrome]] |
- | [[Category: | + | [[Category: Blood coagulation]] |
- | [[Category: | + | [[Category: Cell adhesion]] |
- | [[Category: | + | [[Category: Disease mutation]] |
- | [[Category: | + | [[Category: Glycoprotein]] |
- | [[Category: | + | [[Category: Glycoprotein 1b]] |
- | [[Category: | + | [[Category: Hemostasis]] |
- | [[Category: | + | [[Category: Leucine-rich repeat]] |
- | [[Category: | + | [[Category: Platelet]] |
- | [[Category: | + | [[Category: Polymorphism]] |
- | [[Category: | + | [[Category: Repeat]] |
- | [[Category: | + | [[Category: Signal]] |
- | [[Category: | + | [[Category: Transmembrane]] |
- | [[Category: | + | [[Category: Von willebrand disease]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:05:28 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 15:05, 2 May 2008
STRUCTURE OF GLYCOPROTEIN 1B
Overview
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 anionic region. The structure also demonstrates a novel LRR motif in the form of an M-shaped arrangement of three tandem beta-turns. Negatively charged binding surfaces on the LRR concave face and anionic region indicate two-step binding kinetics to vWF-A1, which can be regulated by an unmasking mechanism involving conformational change of a key loop. Using molecular docking of the GPIb and vWF-A1 crystal structures, we were also able to model the GPIb.vWF-A1 complex.
About this Structure
1GWB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 18:05:28 2008
Categories: Homo sapiens | Single protein | Clemetson, J. | Clemetson, K. | Emsley, J. | Harrison, T. | Uff, S. | Bernard soulier syndrome | Blood coagulation | Cell adhesion | Disease mutation | Glycoprotein | Glycoprotein 1b | Hemostasis | Leucine-rich repeat | Platelet | Polymorphism | Repeat | Signal | Transmembrane | Von willebrand disease