2ayk: Difference between revisions
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[[Image:2ayk.png|left|200px]] | [[Image:2ayk.png|left|200px]] | ||
{{STRUCTURE_2ayk| PDB=2ayk | SCENE= }} | {{STRUCTURE_2ayk| PDB=2ayk | SCENE= }} | ||
===INHIBITOR-FREE CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE, NMR, MINIMIZED AVERAGE STRUCTURE=== | ===INHIBITOR-FREE CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE, NMR, MINIMIZED AVERAGE STRUCTURE=== | ||
{{ABSTRACT_PUBMED_9484219}} | {{ABSTRACT_PUBMED_9484219}} | ||
==About this Structure== | ==About this Structure== | ||
[[2ayk]] is a 1 chain structure of [[Matrix metalloproteinase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AYK OCA]. | |||
==See Also== | |||
*[[Matrix metalloproteinase|Matrix metalloproteinase]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:009484219</ref><ref group="xtra">PMID:012595271</ref><ref group="xtra">PMID:015616985</ref><references group="xtra"/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Interstitial collagenase]] | [[Category: Interstitial collagenase]] | ||
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[[Category: Matrix metalloproteinase]] | [[Category: Matrix metalloproteinase]] | ||
[[Category: Metalloprotease]] | [[Category: Metalloprotease]] | ||
Revision as of 20:11, 25 July 2012
INHIBITOR-FREE CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE, NMR, MINIMIZED AVERAGE STRUCTURE
Template:ABSTRACT PUBMED 9484219
About this Structure
2ayk is a 1 chain structure of Matrix metalloproteinase with sequence from Homo sapiens. Full experimental information is available from OCA.
See Also
Reference
- Moy FJ, Chanda PK, Cosmi S, Pisano MR, Urbano C, Wilhelm J, Powers R. High-resolution solution structure of the inhibitor-free catalytic fragment of human fibroblast collagenase determined by multidimensional NMR. Biochemistry. 1998 Feb 10;37(6):1495-504. PMID:9484219 doi:10.1021/bi972181w
- Kallblad P, Dean PM. Efficient conformational sampling of local side-chain flexibility. J Mol Biol. 2003 Mar 7;326(5):1651-65. PMID:12595271
- Lang A, Csizmadia IG, Perczel A. Peptide models XLV: conformational properties of N-formyl-L-methioninamide and its relevance to methionine in proteins. Proteins. 2005 Feb 15;58(3):571-88. PMID:15616985 doi:10.1002/prot.20307