NDLI: Solution Structures of Ca2+-CIB1 and Mg2+-CIB1 and Their Interactions with the Platelet Integrin αIIb Cytoplasmic Domain*

Content Provider	PubMed Central
Author	Huang, Hao Ishida, Hiroaki Yamniuk, Aaron P. Vogel, Hans J.
Copyright Year	2011
Abstract	The calcium- and integrin-binding protein 1 (CIB1) is a ubiquitous Ca2+-binding protein and a specific binding partner for the platelet integrin αIIb cytoplasmic domain, which confers the key role of CIB1 in hemostasis. CIB1 is also known to be involved in apoptosis, embryogenesis, and the DNA damage response. In this study, the solution structures of both Ca2+-CIB1 and Mg2+-CIB1 were determined using solution-state NMR spectroscopy. The methyl groups of Ile, Leu, and Val were selectively protonated to compensate for the loss of protons due to deuteration. The solution structure of Ca2+-CIB1 possesses smaller opened EF-hands in its C-domain compared with available crystal structures. Ca2+-CIB1 and Mg2+-CIB1 have similar structures, but the N-lobe of Mg2+-CIB1 is slightly more opened than that of Ca2+-CIB1. Additional NMR experiments, such as chemical shift perturbation and methyl group solvent accessibility as measured by a nitroxide surface probe, were carried out to further characterize the structures of Ca2+-CIB1 and Mg2+-CIB1 as well as their interactions with the integrin αIIb cytoplasmic domain. NMR measurements of backbone amide proton slow motion (microsecond to millisecond) dynamics confirmed that the C-terminal helix of Ca2+-CIB1 is displaced upon αIIb binding. The EF-hand III of both Ca2+-CIB1 and Mg2+-CIB1 was identified to be directly involved in the interaction of CIB1 with αIIb. Together, these data illustrate that CIB1 behaves quite differently from related EF-hand regulatory calcium-binding proteins, such as calmodulin or neuronal calcium sensor proteins.
Related Links	http://dx.doi.org/10.1074/jbc.m110.179028
Ending Page	17192
Page Count	12
Starting Page	17181
File Format	PDF
ISSN	00219258
e-ISSN	1083351X
Journal	The Journal of Biological Chemistry
Issue Number	19
Volume Number	286
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2011-05-13
Access Restriction	Open
Rights Holder	American Society for Biochemistry and Molecular Biology
Subject Keyword	Cell Biology Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Solution Structures of Ca2+-CIB1 and Mg2+-CIB1 and Their Interactions with the Platelet Integrin αIIb Cytoplasmic Domain

Solution structures of the cytoplasmic tail complex from platelet integrin αIIb- and β3-subunits

Calcium- and magnesium-dependent interactions between calcium- and integrin-binding protein and the integrin αIIb cytoplasmic domain

Identification of a Novel Calcium-binding Protein That Interacts with the Integrin αIIb Cytoplasmic Domain

Calcium- and magnesium-dependent interactions between calcium- and integrin-binding protein and the integrin αIIb cytoplasmic domain

The Interaction between Calcium- and Integrin-binding Protein 1 and the αIIb Integrin Cytoplasmic Domain Involves a Novel C-terminal Displacement Mechanism

The Interaction of Integrin αIIbβ3 with Fibrin Occurs through Multiple Binding Sites in the αIIb β-Propeller Domain*

Enhancement by Mg2+ of domain specificity in Ca2+-dependent interactions of calmodulin with target sequences.

Direct Binding of the Platelet Integrin αIIbβ3 (GPIIb-IIIa) to Talin EVIDENCE THAT INTERACTION IS MEDIATED THROUGH THE CYTOPLASMIC DOMAINS OF BOTH αIIb AND β3

Solution Structures of Ca2+-CIB1 and Mg2+-CIB1 and Their Interactions with the Platelet Integrin αIIb Cytoplasmic Domain*

Similar Documents

Solution Structures of Ca2+-CIB1 and Mg2+-CIB1 and Their Interactions with the Platelet Integrin αIIb Cytoplasmic Domain

Solution structures of the cytoplasmic tail complex from platelet integrin αIIb- and β3-subunits

Calcium- and magnesium-dependent interactions between calcium- and integrin-binding protein and the integrin αIIb cytoplasmic domain

Identification of a Novel Calcium-binding Protein That Interacts with the Integrin αIIb Cytoplasmic Domain

Calcium- and magnesium-dependent interactions between calcium- and integrin-binding protein and the integrin αIIb cytoplasmic domain

The Interaction between Calcium- and Integrin-binding Protein 1 and the αIIb Integrin Cytoplasmic Domain Involves a Novel C-terminal Displacement Mechanism

The Interaction of Integrin αIIbβ3 with Fibrin Occurs through Multiple Binding Sites in the αIIb β-Propeller Domain*

Enhancement by Mg2+ of domain specificity in Ca2+-dependent interactions of calmodulin with target sequences.

Direct Binding of the Platelet Integrin αIIbβ3 (GPIIb-IIIa) to Talin EVIDENCE THAT INTERACTION IS MEDIATED THROUGH THE CYTOPLASMIC DOMAINS OF BOTH αIIb AND β3

Solution Structures of Ca2+-CIB1 and Mg2+-CIB1 and Their Interactions with the Platelet Integrin αIIb Cytoplasmic Domain*