1av5
From Proteopedia
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==Overview== | ==Overview== | ||
- | The histidine triad (HIT) protein family is among the most ubiquitous and | + | The histidine triad (HIT) protein family is among the most ubiquitous and highly conserved in nature, but a biological activity has not yet been identified for any member of the HIT family. Fragile histidine triad protein (FHIT) and protein kinase C interacting protein (PKCI) were used in a structure-based approach to elucidate characteristics of in vivo ligands and reactions. Crystallographic structures of apo, substrate analog, pentacovalent transition-state analog, and product states of both enzymes reveal a catalytic mechanism and define substrate characteristics required for catalysis, thus unifying the HIT family as nucleotidyl hydrolases, transferases, or both. The approach described here may be useful in identifying structure-function relations between protein families identified through genomics. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
- | [[Category: Hendrickson, W | + | [[Category: Hendrickson, W A.]] |
- | [[Category: Klein, M | + | [[Category: Klein, M G.]] |
- | [[Category: Lima, C | + | [[Category: Lima, C D.]] |
[[Category: AP2]] | [[Category: AP2]] | ||
[[Category: histidine triad protein family]] | [[Category: histidine triad protein family]] | ||
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[[Category: protein kinase inhibitor]] | [[Category: protein kinase inhibitor]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:41 2008'' |
Revision as of 09:48, 21 February 2008
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PKCI-SUBSTRATE ANALOG
Overview
The histidine triad (HIT) protein family is among the most ubiquitous and highly conserved in nature, but a biological activity has not yet been identified for any member of the HIT family. Fragile histidine triad protein (FHIT) and protein kinase C interacting protein (PKCI) were used in a structure-based approach to elucidate characteristics of in vivo ligands and reactions. Crystallographic structures of apo, substrate analog, pentacovalent transition-state analog, and product states of both enzymes reveal a catalytic mechanism and define substrate characteristics required for catalysis, thus unifying the HIT family as nucleotidyl hydrolases, transferases, or both. The approach described here may be useful in identifying structure-function relations between protein families identified through genomics.
About this Structure
1AV5 is a Single protein structure of sequence from Homo sapiens with as ligand. Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.
Reference
Structure-based analysis of catalysis and substrate definition in the HIT protein family., Lima CD, Klein MG, Hendrickson WA, Science. 1997 Oct 10;278(5336):286-90. PMID:9323207
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