TY  - JOUR
AU  - Müller, S.
AU  - Lange, S.
AU  - Gautel, M.
AU  - Wilmanns, M.
AU  - DESY
TI  - Rigid conformation of an immunoglobulin domain tandem repeat in the A-band of the elastic muscle protein titin.
JO  - Journal of molecular biology
VL  - 371
SN  - 0022-2836
CY  - Amsterdam [u.a.]
PB  - Elsevier
M1  - PHPPUBDB-6302
SP  - 480
PY  - 2007
AB  - Most of the structure of the giant muscle protein titin is formed by small modular domains. Many of them are predicted to be arranged in repeats with short linkers that may be key determinants of the peculiar elastic properties of titin. Here, we present the molecular structure of a tandem arrangement of two immunoglobulin-like domains, A168 and A169, located within the A-band segment of titin. The two domains are connected by a 17 residue long beta-strand and form a common interface. Based on these data, we establish general principles to estimate the amount of conformational flexibility of tandem domain motifs in titin. An unusual bulge within the second domain, A169, is directly involved into binding to a sarcomeric ligand, MURF-1, thus suggesting a dual role of this tandem for both the mechanical properties of titin and for sarcomeric signaling.
KW  - Alanine: chemistry
KW  - Amino Acid Sequence
KW  - Conserved Sequence
KW  - Crystallography, X-Ray
KW  - Elasticity
KW  - Humans
KW  - Immunoglobulins: chemistry
KW  - Ligands
KW  - Models, Molecular
KW  - Molecular Sequence Data
KW  - Muscle Proteins: chemistry
KW  - Protein Binding
KW  - Protein Kinases: chemistry
KW  - Protein Structure, Secondary
KW  - Protein Structure, Tertiary
KW  - Sequence Alignment
KW  - Tandem Repeat Sequences
KW  - Immunoglobulins (NLM Chemicals)
KW  - Ligands (NLM Chemicals)
KW  - Muscle Proteins (NLM Chemicals)
KW  - connectin (NLM Chemicals)
KW  - Alanine (NLM Chemicals)
KW  - Protein Kinases (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:17574571
UR  - <Go to ISI:>//WOS:000248509100017
DO  - DOI:10.1016/j.jmb.2007.05.055
UR  - https://bib-pubdb1.desy.de/record/81612
ER  -