1amh
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Structure-based mutational analysis of serine protease specificity has | + | Structure-based mutational analysis of serine protease specificity has produced a large database of information useful in addressing biological function and in establishing a basis for targeted design efforts. Critical issues examined include the function of water molecules in providing strength and specificity of binding, the extent to which binding subsites are interdependent, and the roles of polypeptide chain flexibility and distal structural elements in contributing to specificity profiles. The studies also provide a foundation for exploring why specificity modification can be either straightforward or complex, depending on the particular system. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Trypsin]] | [[Category: Trypsin]] | ||
| - | [[Category: Bocskei, Z | + | [[Category: Bocskei, Z S.]] |
[[Category: Graf, L.]] | [[Category: Graf, L.]] | ||
[[Category: Naray-Szabo, G.]] | [[Category: Naray-Szabo, G.]] | ||
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[[Category: substrate specificity hydrolase]] | [[Category: substrate specificity hydrolase]] | ||
| - | ''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 11:46:07 2008'' |
Revision as of 09:46, 21 February 2008
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UNCOMPLEXED RAT TRYPSIN MUTANT WITH ASP 189 REPLACED WITH SER (D189S)
Overview
Structure-based mutational analysis of serine protease specificity has produced a large database of information useful in addressing biological function and in establishing a basis for targeted design efforts. Critical issues examined include the function of water molecules in providing strength and specificity of binding, the extent to which binding subsites are interdependent, and the roles of polypeptide chain flexibility and distal structural elements in contributing to specificity profiles. The studies also provide a foundation for exploring why specificity modification can be either straightforward or complex, depending on the particular system.
About this Structure
1AMH is a Single protein structure of sequence from Rattus rattus with as ligand. Active as Trypsin, with EC number 3.4.21.4 Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
Structural basis of substrate specificity in the serine proteases., Perona JJ, Craik CS, Protein Sci. 1995 Mar;4(3):337-60. PMID:7795518
Page seeded by OCA on Thu Feb 21 11:46:07 2008
