000081612 001__ 81612
000081612 005__ 20250731125903.0
000081612 0247_ $$2pmid$$apmid:17574571
000081612 0247_ $$2doi$$a10.1016/j.jmb.2007.05.055
000081612 0247_ $$2ISSN$$a1089-8638
000081612 0247_ $$2ISSN$$a0022-2836
000081612 0247_ $$2WOS$$aWOS:000248509100017
000081612 0247_ $$2altmetric$$aaltmetric:42303919
000081612 0247_ $$2openalex$$aopenalex:W1980844103
000081612 037__ $$aPHPPUBDB-6302
000081612 041__ $$aeng
000081612 082__ $$a570
000081612 1001_ $$aMüller, S.
000081612 1101_ $$aDESY$$bEuropean Molecular Biology Laboratory
000081612 245__ $$aRigid conformation of an immunoglobulin domain tandem repeat in the A-band of the elastic muscle protein titin.
000081612 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2007
000081612 300__ $$a480
000081612 3367_ $$00$$2EndNote$$aJournal Article
000081612 3367_ $$2BibTeX$$aARTICLE
000081612 3367_ $$2DRIVER$$aarticle
000081612 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$mjournal
000081612 440_0 $$0PERI:(DE-600)1355192-9$$aJ. Mol. Biol.$$v371$$x0022-2836$$y469
000081612 500__ $$3Converted on 2013-05-30 11:26
000081612 500__ $$3Converted on 2013-06-21 19:20
000081612 520__ $$aMost 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.
000081612 536__ $$0G:(DE-H253)POF1-No-Ref-20130405$$aFS Beamline without reference (POF1-550)$$cPOF1-550$$fPOF I$$x0
000081612 588__ $$aDataset connected to Pubmed
000081612 650_2 $$2MeSH$$aAlanine: chemistry
000081612 650_2 $$2MeSH$$aAmino Acid Sequence
000081612 650_2 $$2MeSH$$aConserved Sequence
000081612 650_2 $$2MeSH$$aCrystallography, X-Ray
000081612 650_2 $$2MeSH$$aElasticity
000081612 650_2 $$2MeSH$$aHumans
000081612 650_2 $$2MeSH$$aImmunoglobulins: chemistry
000081612 650_2 $$2MeSH$$aLigands
000081612 650_2 $$2MeSH$$aModels, Molecular
000081612 650_2 $$2MeSH$$aMolecular Sequence Data
000081612 650_2 $$2MeSH$$aMuscle Proteins: chemistry
000081612 650_2 $$2MeSH$$aProtein Binding
000081612 650_2 $$2MeSH$$aProtein Kinases: chemistry
000081612 650_2 $$2MeSH$$aProtein Structure, Secondary
000081612 650_2 $$2MeSH$$aProtein Structure, Tertiary
000081612 650_2 $$2MeSH$$aSequence Alignment
000081612 650_2 $$2MeSH$$aTandem Repeat Sequences
000081612 650_7 $$00$$2NLM Chemicals$$aImmunoglobulins
000081612 650_7 $$00$$2NLM Chemicals$$aLigands
000081612 650_7 $$00$$2NLM Chemicals$$aMuscle Proteins
000081612 650_7 $$00$$2NLM Chemicals$$aconnectin
000081612 650_7 $$056-41-7$$2NLM Chemicals$$aAlanine
000081612 650_7 $$0EC 2.7.-$$2NLM Chemicals$$aProtein Kinases
000081612 693__ $$0EXP:(DE-H253)Unknown-BL-20150101$$6EXP:(DE-H253)Unknown-BL-20150101$$fUnknown DESY Beamline$$x0
000081612 7001_ $$aLange, S.
000081612 7001_ $$aGautel, M.
000081612 7001_ $$aWilmanns, M.
000081612 773__ $$0PERI:(DE-600)1355192-9$$a10.1016/j.jmb.2007.05.055$$gVol. 371, p. 480$$p480$$q371<480$$tJournal of molecular biology$$v371$$x0022-2836$$y2007
000081612 909CO $$ooai:bib-pubdb1.desy.de:81612$$pVDB
000081612 9101_ $$0I:(DE-HGF)0$$aExternes Institut$$kExtern
000081612 9131_ $$0G:(DE-HGF)POF1-540$$1G:(DE-HGF)POF1-550$$2G:(DE-HGF)POF1-500$$3G:(DE-HGF)POF1$$4G:(DE-HGF)POF$$9G:(DE-H253)POF1-No-Ref-20130405$$aDE-H253$$bStruktur der Materie$$lGroßgeräte für die Forschung mit Photonen, Neutronen, Ionen$$vKondensierte Materie$$x0
000081612 9141_ $$a(c) Elsevier. No copyright permission for full text.$$y2007
000081612 915__ $$0StatID:(DE-HGF)0010$$2StatID$$aJCR/ISI refereed
000081612 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR
000081612 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection
000081612 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bThomson Reuters Master Journal List
000081612 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline
000081612 915__ $$0StatID:(DE-HGF)1$$2StatID$$aNo Author Disambiguation
000081612 920_1 $$iEuropean Molecular Biology Laboratory$$kEMBL
000081612 9201_ $$0I:(DE-H253)EMBL_-2012_-20130307$$kEMBL$$lEuropean Molecular Biology Laboratory$$x0
000081612 920__ $$k001
000081612 980__ $$aPHPPUBDB
000081612 980__ $$aVDB
000081612 980__ $$aUNRESTRICTED
000081612 980__ $$ajournal
000081612 980__ $$aI:(DE-H253)EMBL_-2012_-20130307
000081612 980__ $$aConvertedRecord