Crystal structure of the wild-type von Willebrand factor A1-glycoprotein Ibalpha complex reveals conformation differences with a complex bearing von Willebrand disease mutations (Q24319306)

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English	Crystal structure of the wild-type von Willebrand factor A1-glycoprotein Ibalpha complex reveals conformation differences with a complex bearing von Willebrand disease mutations	scientific article

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Crystal structure of the wild-type von Willebrand factor A1-glycoprotein Ibalpha complex reveals conformation differences with a complex bearing von Willebrand disease mutations (English)

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crystal structure

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author name string

John J Dumas

1

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Ravindra Kumar

2

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Thomas McDonagh

3

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Francis Sullivan

4

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Mark L Stahl

5

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William S Somers

6

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Lidia Mosyak

7

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language of work or name

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publication date

28 May 2004

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Journal of Biological Chemistry

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279

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22

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23327-34

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Biochemistry and genetics of von Willebrand factor

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Molecular mechanisms of platelet adhesion and activation

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Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor

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Human blood platelets showing no response to collagen fail to express surface glycoprotein Ia

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Collagen receptor signalling in platelets: extending the role of the ITAM.

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Specific synergy of multiple substrate-receptor interactions in platelet thrombus formation under flow.

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Distinct abnormalities in the interaction of purified types IIA and IIB von Willebrand factor with the two platelet binding sites, glycoprotein complexes Ib-IX and IIb-IIIa

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Interaction of purified type IIB von Willebrand factor with the platelet membrane glycoprotein Ib induces fibrinogen binding to the glycoprotein IIb/IIIa complex and initiates aggregation

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Von Willebrand factor and von Willebrand disease

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Molecular basis of von Willebrand disease type IIB. Candidate mutations cluster in one disulfide loop between proposed platelet glycoprotein Ib binding sequences

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Low shear stress can initiate von Willebrand factor-dependent platelet aggregation in patients with type IIB and platelet-type von Willebrand disease

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Identification of aspartic acid 514 through glutamic acid 542 as a glycoprotein Ib-IX complex receptor recognition sequence in von Willebrand factor. Mechanism of modulation of von Willebrand factor by ristocetin and botrocetin

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Pseudo-von Willebrand's disease. An intrinsic platelet defect with aggregation by unmodified human factor VIII/von Willebrand factor and enhanced adsorption of its high-molecular-weight multimers

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Selectin-like kinetics and biomechanics promote rapid platelet adhesion in flow: the GPIb(alpha)-vWF tether bond

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Alterations in the intrinsic properties of the GPIbalpha-VWF tether bond define the kinetics of the platelet-type von Willebrand disease mutation, Gly233Val

1 reference

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Crystal structure of the von Willebrand Factor A1 domain and implications for the binding of platelet glycoprotein Ib

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Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain

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Identification of amino acid residues essential for von Willebrand factor binding to platelet glycoprotein Ib. Charged-to-alanine scanning mutagenesis of the A1 domain of human von Willebrand factor

1 reference

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Epitope mapping of inhibitory antibodies against platelet glycoprotein Ibalpha reveals interaction between the leucine-rich repeat N-terminal and C-terminal flanking domains of glycoprotein Ibalpha.

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von Willebrand factor conformation and adhesive function is modulated by an internalized water molecule

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Processing of X-ray diffraction data collected in oscillation mode

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The CCP4 suite: programs for protein crystallography

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https://api.crossref.org/works/10.1074%2FJBC.M401659200

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[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods.

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https://api.crossref.org/works/10.1074%2FJBC.M401659200

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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Tyrosine sulfation of the glycoprotein Ib-IX complex: identification of sulfated residues and effect on ligand binding

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Identification of three tyrosine residues of glycoprotein Ib alpha with distinct roles in von Willebrand factor and alpha-thrombin binding

1 reference

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Structural basis of von Willebrand factor activation by the snake toxin botrocetin

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Accommodating sequence changes in beta-hairpins in proteins

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Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

1 reference

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Distinct structural attributes regulating von Willebrand factor A1 domain interaction with platelet glycoprotein Ibalpha under flow

1 reference

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Modulation of alpha-thrombin function by distinct interactions with platelet glycoprotein Ibalpha

1 reference

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Crystal structure of the GpIbalpha-thrombin complex essential for platelet aggregation

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Beta-and gamma-turns in proteins revisited: a new set of amino acid turn-type dependent positional preferences and potentials

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based on heuristic

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One type of gamma-turn, rather than the other gives rise to chain-reversal in proteins

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based on heuristic

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Cross-linking of a monomeric 39/34-kDa dispase fragment of von Willebrand factor (Leu-480/Val-481-Gly-718) to the N-terminal region of the alpha-chain of membrane glycoprotein Ib on intact platelets with bis(sulfosuccinimidyl) suberate

1 reference

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7 January 2021

based on heuristic

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Mocarhagin, a novel cobra venom metalloproteinase, cleaves the platelet von Willebrand factor receptor glycoprotein Ibalpha. Identification of the sulfated tyrosine/anionic sequence Tyr-276-Glu-282 of glycoprotein Ibalpha as a binding site for von W

1 reference

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7 January 2021

based on heuristic

inferred from DOI database lookup

Heightened interaction between platelets and factor VIII/von Willebrand factor in a new subtype of von Willebrand's disease

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https://api.crossref.org/works/10.1074%2FJBC.M401659200

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based on heuristic

inferred from DOI database lookup

Interaction of von Willebrand Factor Domain A1 with Platelet Glycoprotein Ibα-(1–289)

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https://api.crossref.org/works/10.1074%2FJBC.M401659200

7 January 2021

based on heuristic

inferred from DOI database lookup

Von Willebrand factor

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7 January 2021

based on heuristic

inferred from DOI database lookup

Identifiers

10.1074/JBC.M401659200

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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