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Volumn 129, Issue 19, 2007, Pages 6140-6148

Protein design: Reengineering Cellular Retinoic Acid Binding Protein II into a rhodopsin protein mimic

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR RETINOIC ACID BINDING PROTEIN II (CRABPII); IMINE; NANOMOLAR BINDING; SCHIFF BASE;

EID: 34249040518     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja067546r     Document Type: Article
Times cited : (43)

References (93)
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    • (1983) Science , vol.219 , pp. 666-671
    • Ulmer, K.M.1
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    • 4043174875 scopus 로고    scopus 로고
    • Improving the functional expression of N-carbamoylase by directed evolution using the green fluorescent protein fusion reporter system
    • Academic Press
    • Park, H. S.; Oh, K. H.; Kim, H. S. Improving the functional expression of N-carbamoylase by directed evolution using the green fluorescent protein fusion reporter system. Methods in Enzymology; Academic Press: 2004; Vol. 388, pp 187-195.
    • (2004) Methods in Enzymology , vol.388 , pp. 187-195
    • Park, H.S.1    Oh, K.H.2    Kim, H.S.3
  • 18
    • 0037844721 scopus 로고    scopus 로고
    • DeGrado, W. F. Nature 2003, 423, 132-133.
    • (2003) Nature , vol.423 , pp. 132-133
    • DeGrado, W.F.1
  • 81
    • 34249004443 scopus 로고    scopus 로고
    • The active site water residue in all crystal structures in this manuscript are labeled as W1 to indicate the fact that they are all in the same position. The actual water numbering of W1 in the PDB files for each mutant is as follows: wild type CRABPII bound to RA (1CBS, W309), R132K:Y134F-CRABPII bound to RA (2G78, W11), R132K:Y134F-CRABPII bound to RT (2G79, W10).
    • The active site water residue in all crystal structures in this manuscript are labeled as W1 to indicate the fact that they are all in the same position. The actual water numbering of W1 in the PDB files for each mutant is as follows: wild type CRABPII bound to RA (1CBS, W309), R132K:Y134F-CRABPII bound to RA (2G78, W11), R132K:Y134F-CRABPII bound to RT (2G79, W10).
  • 84
    • 34249065990 scopus 로고    scopus 로고
    • Crystal structure of L121E mutants bound to retinoic acid (unpublished results) exhibit a bis-carboxylic acid dimer, formed between the Glu121 and retinoic acid. The geometry and distance between the tightly hydrogen bonded carboxylic acids is suggestive of the fact that Glu121 is protonated.
    • Crystal structure of L121E mutants bound to retinoic acid (unpublished results) exhibit a bis-carboxylic acid dimer, formed between the Glu121 and retinoic acid. The geometry and distance between the tightly hydrogen bonded carboxylic acids is suggestive of the fact that Glu121 is protonated.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.