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Volumn 317, Issue 2, 2002, Pages 279-290

A structural basis for S100 protein specificity derived from comparative analysis of apo and Ca2+-calcyclin

Author keywords

Ca2+ binding protein; Calcyclin; EF hand; Nuclear magnetic resonance; S100 protein

Indexed keywords

ANNEXIN; BINDING PROTEIN; CALCIUM; CALCIUM BINDING PROTEIN; CALCYCLIN; CALMODULIN; NERVE PROTEIN; PROTEIN S 100; PROTEIN S100B;

EID: 0036296180     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2002.5421     Document Type: Article
Times cited : (48)

References (53)
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    • A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form
    • (1998) Structure , vol.6 , pp. 211-2222
    • Smith, S.P.1    Shaw, G.S.2
  • 20
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    • Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA
    • (1991) J. Mol. Biol. , vol.217 , pp. 517-530
    • Güntert, P.1    Braun, W.2    Wüthrich, K.3
  • 50
    • 0026259488 scopus 로고
    • Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints
    • (1991) J. Biomol. NMR , vol.1 , pp. 447-456
    • Güntert, P.1    Wüthrich, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.