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Volumn 284, Issue 37, 2009, Pages 25290-25301

The crystal structure of an algal prolyl 4-hydroxylase complexed with a proline-rich peptide reveals a novel buried tripeptide binding motif

Author keywords

[No Author keywords available]

Indexed keywords

2-OXOGLUTARATE; AROMATIC RESIDUES; BINDING MOTIF; CATALYTIC CYCLES; CATALYTIC DOMAINS; CELL-WALL COMPONENTS; CHLAMYDOMONAS REINHARDTII; CONFORMATIONAL CHANGE; CONFORMATIONAL SWITCHES; HYDROXYLASES; HYPOXIA-INDUCIBLE FACTORS; KEY ENZYMES; KEY FEATURE; L-PROLINE; MODE OF BINDING; MONOMERIC ENZYMES; OXYGEN-SENSING; PEPTIDE BINDING; PEPTIDE SUBSTRATES; PROLINE RESIDUES; PROLYL-4-HYDROXYLASE; SEQUENCE SIMILARITY; SIDE CHAINS; SPECIFIC BINDING; STACKING INTERACTION; TERNARY COMPLEX; TRIPEPTIDE; TYPE II;

EID: 69949136771     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.014050     Document Type: Article
Times cited : (58)

References (48)
  • 22
    • 0003076963 scopus 로고
    • Joint CCP4 ESF-EACBM Newsl
    • Leslie, A. G. W. (1992) Joint CCP4 ESF-EACBM Newsl. Protein Crystallogr. 26, 22-33
    • (1992) Protein Crystallogr , vol.26 , pp. 22-33
    • Leslie, A.G.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.