NDLI: $^{1}$H, $^{15}$N and $^{13}$C backbone chemical shift assignment of titin domains A59

Content Provider	Springer Nature Link
Author	Czajlik, András Thompson, Gary S. Khan, Ghulam N. Kalverda, Arut P. Homans, Steve W. Trinick, John
Copyright Year	2014
Abstract	The giant protein titin is the third most abundant protein of vertebrate striated muscle. The titin molecule is >1 μm long and spans half the sarcomere, from the Z-disk to the M-line, and has important roles in sarcomere assembly, elasticity and intracellular signaling. In the A-band of the sarcomere titin is attached to the thick filaments and mainly consists immunoglobulin-like and fibronectin type III-like domains. These are mostly arranged in long-range patterns or ‘super-repeats’. The large super-repeats each contain 11 domains and are repeated 11 times, thus forming nearly half the titin molecule. Through interactions with myosin and C-protein, they are involved in thick filament assembly. The importance of titin in muscle assembly is highlighted by the effect of mutations in the A-band portion, which are the commonest cause of dilated cardiomyopathy, affecting ~1 in 250 (Herman et al. in N Engl J Med 366:619–628, 2012). Here we report backbone $^{15}$N, $^{13}$C and $^{1}$H chemical shift and $^{13}$Cβ assignments for the A59–A60 domain tandem from the titin A59–A69 large super-repeat, completed using triple resonance NMR. Since, some regions of the backbone remained unassigned in A60 domain of the complete A59–A60 tandem, a construct containing a single A60 domain, A60sd, was also studied using the same methods. Considerably improved assignment coverage was achieved using A60sd due to its lower mass and improved molecular tumbling rate; these assignments also allowed the analysis of inter-domain interactions using chemical shift mapping against A59–A60.
Starting Page	429
Ending Page	433
Page Count	5
File Format	PDF
ISSN	18742718
Journal	Biomolecular NMR Assignments
Volume Number	8
Issue Number	2
e-ISSN	1874270X
Language	English
Publisher	Springer Netherlands
Publisher Date	2014-01-28
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Muscle protein Titin A-band Large super-repeat unit Fibronectin type III domain tandem Biophysics and Biological Physics Polymer Sciences Biochemistry
Content Type	Text
Resource Type	Article
Subject	Structural Biology Biochemistry

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

1H, 15N and 13C backbone chemical shift assignment of titin domains A59–A60 and A60 alone

$^{1}$H, $^{15}$N and $^{13}$C backbone chemical shift assignment of the titin A67-A68 domain tandem

1H, 15N and 13C backbone chemical shift assignment of titin domains A59–A60 and A60 alone

Sequence-specific $^{1}$H, $^{13}$C and $^{15}$N backbone resonance assignments of the plakin repeat domain of human envoplakin

Letter to the Editor: $^{1}$H, $^{13}$C, and $^{15}$N backbone assignment of the first two Ig domains Z1Z2 of the giant muscle protein Titin

Sequence-specific $^{1}$H, $^{13}$C, and $^{15}$N backbone assignment of the 28 kDa PDZ2/PDZ3 tandem domain of the protein tyrosine phosphatase PTP-BL

$^{1}$H, $^{13}$C and $^{15}$N Backbone Resonance Assignment of the Hsp90 Binding Domain of Human Cdc37

$^{1}$H, $^{13}$C and $^{15}$N backbone assignment of the EC-1 domain of human E-cadherin

$^{1}$H, $^{13}$C, and $^{15}$N backbone and sidechain chemical shift assignments for the HEAT2 domain of human eIF4GI

$^{1}$H, $^{15}$N and $^{13}$C backbone chemical shift assignment of titin domains A59–A60 and A60 alone

Similar Documents

1H, 15N and 13C backbone chemical shift assignment of titin domains A59–A60 and A60 alone

$^{1}$H, $^{15}$N and $^{13}$C backbone chemical shift assignment of the titin A67-A68 domain tandem

1H, 15N and 13C backbone chemical shift assignment of titin domains A59–A60 and A60 alone

Sequence-specific $^{1}$H, $^{13}$C and $^{15}$N backbone resonance assignments of the plakin repeat domain of human envoplakin

Letter to the Editor: $^{1}$H, $^{13}$C, and $^{15}$N backbone assignment of the first two Ig domains Z1Z2 of the giant muscle protein Titin

Sequence-specific $^{1}$H, $^{13}$C, and $^{15}$N backbone assignment of the 28 kDa PDZ2/PDZ3 tandem domain of the protein tyrosine phosphatase PTP-BL

$^{1}$H, $^{13}$C and $^{15}$N Backbone Resonance Assignment of the Hsp90 Binding Domain of Human Cdc37

$^{1}$H, $^{13}$C and $^{15}$N backbone assignment of the EC-1 domain of human E-cadherin

$^{1}$H, $^{13}$C, and $^{15}$N backbone and sidechain chemical shift assignments for the HEAT2 domain of human eIF4GI

$^{1}$H, $^{15}$N and $^{13}$C backbone chemical shift assignment of titin domains A59–A60 and A60 alone