Structural and energetic aspects of protein-protein recognition

• Autorzy: Otlewski J. , Apostoluk W.
• Języki publikacji: EN

Abstrakty

EN

Specific recognition between proteins plays a crucial role in a great number of vital processes. In this review different types of protein-protein complexes are analyzed on the basis of their three-dimensional structures which became available in recent years. The complexes which are analyzed include: those resulting from different types of recognition between proteinase and protein inhibitor (canonical inhibitors of serine proteinases, hirudin, inhibitors of cysteine proteinases, carboxypeptidase inhibitor), barnase-barstar, human growth hormone-receptor and antibody-antigen. It seems obvious that specific and strong protein-protein recognition is achieved in many different ways. To further explore this question, the structural information was analyzed together with kinetic and thermodynamic data available for the respective complexes. It appears that the energy and rates of specific recognition of proteins are influenced by many different factors, including: area of interacting surfaces; complementarity of shapes, charges and hydrogen bonds; water structure at the interface; conformational changes; additivity and cooperativity of individ­ual interactions, steric effects and various (conformational, hydration) entropy changes.

Słowa kluczowe

EN

thrombin-hirudin interaction; protein-protein complex; barnase; barnase-barstar complex; antibody; serine proteinase; antigen; receptor; recognition; protein; inhibitor; barstar; hormone

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1997
• Tom: 44
• Numer: 3
• Opis fizyczny: p.367-387,fig.

Twórcy

autor

Otlewski J.

• University of Wroclaw, Tamka 2, PL-50-137 Wroclaw, Poland, E-mail: [e-mail]

autor

Apostoluk W.

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