PDBsum entry 5joe

Transferase

PDB id

5joe

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Contents

			Protein chain

					92 a.a.

			Ligands

					IPA


					EDO

			Waters ×179

PDB id:

5joe

Links

Name:

Transferase

Title:

Crystal structure of i81 from titin

Structure:

Titin. Chain: a. Fragment: i81 domain. Synonym: connectin,rhabdomyosarcoma antigen mu-rms-40.14. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ttn. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.00Å

R-factor:

0.179

R-free:

0.218

Authors:

J.Fleming,T.Zhou,J.Bogomolovas,S.Labeit,O.Mayans

Key ref:

T.Zhou et al. (2016). CARP interacts with titin at a unique helical N2A sequence and at the domain Ig81 to form a structured complex. Febs Lett, 590, 3098-3110. PubMed id: 27531639 DOI: 10.1002/1873-3468.12362

Date:

02-May-16

Release date:

17-Aug-16

PROCHECK

	Headers

	References

Protein chain

Q8WZ42 (TITIN_HUMAN) - Titin from Homo sapiens

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Seq: Struc:					34350 a.a. 92 a.a.*

Key:

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 2 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

E.C.2.7.11.1 - non-specific serine/threonine protein kinase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

1.	L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
2.	L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺

L-seryl-[protein]	+	ATP	=	O-phospho-L-seryl-[protein]	+	ADP	+	H(+)

L-threonyl-[protein]	+	ATP	=	O-phospho-L-threonyl-[protein]	+	ADP	+	H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1002/1873-3468.12362	Febs Lett 590:3098-3110 (2016)
PubMed id: 27531639

CARP interacts with titin at a unique helical N2A sequence and at the domain Ig81 to form a structured complex.
T.Zhou, J.R.Fleming, B.Franke, J.Bogomolovas, I.Barsukov, D.J.Rigden, S.Labeit, O.Mayans.

ABSTRACT

The cardiac ankyrin repeat protein (CARP) is up-regulated in the myocardium during cardiovascular disease and in response to mechanical or toxic stress. Stress-induced CARP interacts with the N2A spring region of the titin filament to modulate muscle compliance. We characterize the interaction between CARP and titin-N2A and show that the binding site in titin spans the dual domain UN2A-Ig81. We find that the unique sequence UN2A is not structurally disordered, but that it has a stable, elongated α-helical fold that possibly acts as a constant force spring. Our findings portray CARP/titin-N2A as a structured node and help to rationalize the molecular basis of CARP mechanosensing in the sarcomeric I-band.