guest ::
| Home > Publications database > Rigid conformation of an immunoglobulin domain tandem repeat in the A-band of the elastic muscle protein titin. > print |
| Home > Publications database > Rigid conformation of an immunoglobulin domain tandem repeat in the A-band of the elastic muscle protein titin. > print |
| 001 | 81612 | ||
| 005 | 20250731125903.0 | ||
| 024 | 7 | _ | |a pmid:17574571 |2 pmid |
| 024 | 7 | _ | |a 10.1016/j.jmb.2007.05.055 |2 doi |
| 024 | 7 | _ | |a 1089-8638 |2 ISSN |
| 024 | 7 | _ | |a 0022-2836 |2 ISSN |
| 024 | 7 | _ | |a WOS:000248509100017 |2 WOS |
| 024 | 7 | _ | |a altmetric:42303919 |2 altmetric |
| 024 | 7 | _ | |a openalex:W1980844103 |2 openalex |
| 037 | _ | _ | |a PHPPUBDB-6302 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Müller, S. |
| 110 | 1 | _ | |a DESY |b European Molecular Biology Laboratory |
| 245 | _ | _ | |a Rigid conformation of an immunoglobulin domain tandem repeat in the A-band of the elastic muscle protein titin. |
| 260 | _ | _ | |a Amsterdam [u.a.] |b Elsevier |c 2007 |
| 300 | _ | _ | |a 480 |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Journal Article |m journal |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 440 | _ | 0 | |a J. Mol. Biol. |v 371 |y 469 |x 0022-2836 |0 PERI:(DE-600)1355192-9 |
| 500 | _ | _ | |3 Converted on 2013-05-30 11:26 |
| 500 | _ | _ | |3 Converted on 2013-06-21 19:20 |
| 520 | _ | _ | |a 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. |
| 536 | _ | _ | |0 G:(DE-H253)POF1-No-Ref-20130405 |f POF I |x 0 |c POF1-550 |a FS Beamline without reference (POF1-550) |
| 588 | _ | _ | |a Dataset connected to Pubmed |
| 650 | _ | 2 | |2 MeSH |a Alanine: chemistry |
| 650 | _ | 2 | |2 MeSH |a Amino Acid Sequence |
| 650 | _ | 2 | |2 MeSH |a Conserved Sequence |
| 650 | _ | 2 | |2 MeSH |a Crystallography, X-Ray |
| 650 | _ | 2 | |2 MeSH |a Elasticity |
| 650 | _ | 2 | |2 MeSH |a Humans |
| 650 | _ | 2 | |2 MeSH |a Immunoglobulins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Ligands |
| 650 | _ | 2 | |2 MeSH |a Models, Molecular |
| 650 | _ | 2 | |2 MeSH |a Molecular Sequence Data |
| 650 | _ | 2 | |2 MeSH |a Muscle Proteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Protein Binding |
| 650 | _ | 2 | |2 MeSH |a Protein Kinases: chemistry |
| 650 | _ | 2 | |2 MeSH |a Protein Structure, Secondary |
| 650 | _ | 2 | |2 MeSH |a Protein Structure, Tertiary |
| 650 | _ | 2 | |2 MeSH |a Sequence Alignment |
| 650 | _ | 2 | |2 MeSH |a Tandem Repeat Sequences |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Immunoglobulins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Ligands |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Muscle Proteins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a connectin |
| 650 | _ | 7 | |0 56-41-7 |2 NLM Chemicals |a Alanine |
| 650 | _ | 7 | |0 EC 2.7.- |2 NLM Chemicals |a Protein Kinases |
| 693 | _ | _ | |0 EXP:(DE-H253)Unknown-BL-20150101 |f Unknown DESY Beamline |x 0 |6 EXP:(DE-H253)Unknown-BL-20150101 |
| 700 | 1 | _ | |a Lange, S. |
| 700 | 1 | _ | |a Gautel, M. |
| 700 | 1 | _ | |a Wilmanns, M. |
| 773 | _ | _ | |0 PERI:(DE-600)1355192-9 |a 10.1016/j.jmb.2007.05.055 |g Vol. 371, p. 480 |p 480 |q 371<480 |t Journal of molecular biology |v 371 |x 0022-2836 |y 2007 |
| 909 | C | O | |o oai:bib-pubdb1.desy.de:81612 |p VDB |
| 910 | 1 | _ | |0 I:(DE-HGF)0 |a Externes Institut |k Extern |
| 913 | 1 | _ | |0 G:(DE-HGF)POF1-540 |9 G:(DE-H253)POF1-No-Ref-20130405 |v Kondensierte Materie |x 0 |a DE-H253 |4 G:(DE-HGF)POF |1 G:(DE-HGF)POF1-550 |3 G:(DE-HGF)POF1 |2 G:(DE-HGF)POF1-500 |b Struktur der Materie |l Großgeräte für die Forschung mit Photonen, Neutronen, Ionen |
| 914 | 1 | _ | |a (c) Elsevier. No copyright permission for full text. |y 2007 |
| 915 | _ | _ | |a JCR/ISI refereed |0 StatID:(DE-HGF)0010 |2 StatID |
| 915 | _ | _ | |a JCR |0 StatID:(DE-HGF)0100 |2 StatID |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0150 |2 StatID |b Web of Science Core Collection |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0199 |2 StatID |b Thomson Reuters Master Journal List |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0300 |2 StatID |b Medline |
| 915 | _ | _ | |a No Author Disambiguation |0 StatID:(DE-HGF)1 |2 StatID |
| 920 | _ | 1 | |k EMBL |i European Molecular Biology Laboratory |
| 920 | 1 | _ | |0 I:(DE-H253)EMBL_-2012_-20130307 |k EMBL |l European Molecular Biology Laboratory |x 0 |
| 920 | _ | _ | |k 001 |
| 980 | _ | _ | |a PHPPUBDB |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a UNRESTRICTED |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a I:(DE-H253)EMBL_-2012_-20130307 |
| 980 | _ | _ | |a ConvertedRecord |
| Library | Collection | CLSMajor | CLSMinor | Language | Author |
|---|